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Volumn 33, Issue 1, 2015, Pages 80-116

Recent advances in food biopeptides: Production, biological functionalities and therapeutic applications

Author keywords

Antihypertensive; Antioxidative; Enzymatic hydrolysis; Functional peptides; In vitro and in vivo assessments; Multiple biological activities; Penetration routes; Peptides bioavailability; Protein hydrolysates

Indexed keywords

BIOACTIVITY; BIOCHEMISTRY; HEALTH RISKS; HYDROLYSIS; MOLECULAR BIOLOGY; PEPTIDES; PROTEINS;

EID: 84922858362     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2014.12.003     Document Type: Review
Times cited : (166)

References (419)
  • 1
    • 0344117604 scopus 로고    scopus 로고
    • Functional properties of dietary fibre prepared from defatted rice bran
    • Abdul-Hamid A., Luan Y.S. Functional properties of dietary fibre prepared from defatted rice bran. Food Chem 2000, 68:15-19.
    • (2000) Food Chem , vol.68 , pp. 15-19
    • Abdul-Hamid, A.1    Luan, Y.S.2
  • 3
    • 33645376731 scopus 로고    scopus 로고
    • Nutrigenomics: From molecular nutrition to prevention of disease
    • Afman L., Müller M. Nutrigenomics: From molecular nutrition to prevention of disease. J Am Diet Assoc 2006, 106:569-576.
    • (2006) J Am Diet Assoc , vol.106 , pp. 569-576
    • Afman, L.1    Müller, M.2
  • 4
    • 78651486207 scopus 로고    scopus 로고
    • Insulation of a synthetic hydrogen metabolism circuit in bacteria
    • Agapakis C., Ducat D., Boyle P., Wintermute E., Way J., Silver P. Insulation of a synthetic hydrogen metabolism circuit in bacteria. J Biol Eng 2010, 4(3):2166-2178.
    • (2010) J Biol Eng , vol.4 , Issue.3 , pp. 2166-2178
    • Agapakis, C.1    Ducat, D.2    Boyle, P.3    Wintermute, E.4    Way, J.5    Silver, P.6
  • 5
    • 84856562585 scopus 로고    scopus 로고
    • Rethinking food-derived bioactive peptides for antimicrobial and immunomodulatory activities
    • Agyei D., Danquah M.K. Rethinking food-derived bioactive peptides for antimicrobial and immunomodulatory activities. Trends Food Sci Technol 2011, 10.1016/j.tifs.2011.08.010.
    • (2011) Trends Food Sci Technol
    • Agyei, D.1    Danquah, M.K.2
  • 6
    • 78049439696 scopus 로고    scopus 로고
    • Contribution of Leu and Hyp residues to antioxidant and ACE-inhibitory activities of peptide sequences isolated from squid gelatin hydrolysate
    • Alemán A., Giménez B., Pérez-Santin E., Gómez-Guillén M.C., Montero P. Contribution of Leu and Hyp residues to antioxidant and ACE-inhibitory activities of peptide sequences isolated from squid gelatin hydrolysate. Food Chem 2011, 125:334-341.
    • (2011) Food Chem , vol.125 , pp. 334-341
    • Alemán, A.1    Giménez, B.2    Pérez-Santin, E.3    Gómez-Guillén, M.C.4    Montero, P.5
  • 7
    • 84859078384 scopus 로고    scopus 로고
    • Chapter 24. Controlled release and delivery technology of biologically active proteins and peptides
    • John Wiley's and Sons, USA, IFT Press, Y. Mine, E. Li-Chan, B. Jiang (Eds.)
    • Amar-Yuli I., Aserin A., Garti N. Chapter 24. Controlled release and delivery technology of biologically active proteins and peptides. Bioactive proteins and peptides vas functional foods and nutraceuticals 2010, 359-382. John Wiley's and Sons, USA, IFT Press. Y. Mine, E. Li-Chan, B. Jiang (Eds.).
    • (2010) Bioactive proteins and peptides vas functional foods and nutraceuticals , pp. 359-382
    • Amar-Yuli, I.1    Aserin, A.2    Garti, N.3
  • 8
    • 4344615913 scopus 로고    scopus 로고
    • Anti-HSV activity of lactoferrin and lactoferricin is dependent on the presence of heparan sulphate at the cell surface
    • Andersen J.H., Jenssen H., Sandvik K., Gutteberg T.J. Anti-HSV activity of lactoferrin and lactoferricin is dependent on the presence of heparan sulphate at the cell surface. J Med Virol 2004, 74(2):262-271.
    • (2004) J Med Virol , vol.74 , Issue.2 , pp. 262-271
    • Andersen, J.H.1    Jenssen, H.2    Sandvik, K.3    Gutteberg, T.J.4
  • 9
    • 0036232442 scopus 로고    scopus 로고
    • Purification, characterization, and biological activity of insulins from the spotted dogfish, Scyliorhinus canicula, and the hammerhead shark, Sphyrna lewini
    • Anderson W.G., Ali M.F., Einarsdóttir I.E., Schäffer L., Hazon N., Conlon J.M. Purification, characterization, and biological activity of insulins from the spotted dogfish, Scyliorhinus canicula, and the hammerhead shark, Sphyrna lewini. Gen Comp Endocrinol 2002, 126:113-122.
    • (2002) Gen Comp Endocrinol , vol.126 , pp. 113-122
    • Anderson, W.G.1    Ali, M.F.2    Einarsdóttir, I.E.3    Schäffer, L.4    Hazon, N.5    Conlon, J.M.6
  • 10
    • 1542509435 scopus 로고    scopus 로고
    • Bioactive peptides from marine sources: pharmacological properties and isolation procedures
    • Aneiros A., Garateix A. Bioactive peptides from marine sources: pharmacological properties and isolation procedures. J Chromatogr B 2004, 803:41-53.
    • (2004) J Chromatogr B , vol.803 , pp. 41-53
    • Aneiros, A.1    Garateix, A.2
  • 12
    • 0027596904 scopus 로고
    • Angiotensin-converting enzyme inhibitors derived from food proteins
    • Ariyoshi Y. Angiotensin-converting enzyme inhibitors derived from food proteins. Trends Food Sci Technol 1993, 4(5):139-144.
    • (1993) Trends Food Sci Technol , vol.4 , Issue.5 , pp. 139-144
    • Ariyoshi, Y.1
  • 14
    • 33846697048 scopus 로고    scopus 로고
    • Anticoagulant activity of marine green and brown algae collected from Jeju Island in Korea
    • Athukorala Y., Lee K.W., Kim S.K., Jeon Y.J. Anticoagulant activity of marine green and brown algae collected from Jeju Island in Korea. Bioresour Technol 2007, 98:1711-1716.
    • (2007) Bioresour Technol , vol.98 , pp. 1711-1716
    • Athukorala, Y.1    Lee, K.W.2    Kim, S.K.3    Jeon, Y.J.4
  • 15
    • 33644860341 scopus 로고    scopus 로고
    • Recent bio-applications of sol-gel materials
    • Avnir D., Lev O., Livage J. Recent bio-applications of sol-gel materials. J Mater Chem 2006, 16:1013-1030.
    • (2006) J Mater Chem , vol.16 , pp. 1013-1030
    • Avnir, D.1    Lev, O.2    Livage, J.3
  • 16
    • 84858161226 scopus 로고    scopus 로고
    • Developmental origins of chronic disease
    • Barker D.J.P. Developmental origins of chronic disease. Public Health 2012, 126:185-189.
    • (2012) Public Health , vol.126 , pp. 185-189
    • Barker, D.J.P.1
  • 17
    • 0031193859 scopus 로고    scopus 로고
    • Peptide stability in solids and solutions
    • Bell L.N. Peptide stability in solids and solutions. Biotechnol Prog 1997, 13(4):342-346.
    • (1997) Biotechnol Prog , vol.13 , Issue.4 , pp. 342-346
    • Bell, L.N.1
  • 20
    • 78751646975 scopus 로고    scopus 로고
    • Isolation, purification of antioxidant peptidic fractions from a bovine liver sarcoplasmic protein thermolysin hydrolysate
    • Bernardini D., Rai D.K., Bolton D., Kerry J., O'Neill E., Mullen A.M., Harnedy P., Hayes M. Isolation, purification of antioxidant peptidic fractions from a bovine liver sarcoplasmic protein thermolysin hydrolysate. Peptides 2011, 32(2):388-400.
    • (2011) Peptides , vol.32 , Issue.2 , pp. 388-400
    • Bernardini, D.1    Rai, D.K.2    Bolton, D.3    Kerry, J.4    O'Neill, E.5    Mullen, A.M.6    Harnedy, P.7    Hayes, M.8
  • 21
    • 51249110348 scopus 로고    scopus 로고
    • Bioinspired enzyme encapsulation for biocatalysis
    • Betancor L., Luckarift H.R. Bioinspired enzyme encapsulation for biocatalysis. Trends Biotechnol 2008, 26:566-572.
    • (2008) Trends Biotechnol , vol.26 , pp. 566-572
    • Betancor, L.1    Luckarift, H.R.2
  • 22
    • 41949086504 scopus 로고    scopus 로고
    • Improving oral bioavailability of peptides by multiple N-methylation: somatostatin analogues
    • Biron E., Chatterjee J., avadioa O., Langenegger J., Brueggen J., Hoyer D., et al. Improving oral bioavailability of peptides by multiple N-methylation: somatostatin analogues. Angew Chem Int Ed 2008, 47:2595-2599.
    • (2008) Angew Chem Int Ed , vol.47 , pp. 2595-2599
    • Biron, E.1    Chatterjee, J.2    avadioa, O.3    Langenegger, J.4    Brueggen, J.5    Hoyer, D.6
  • 23
    • 0043234241 scopus 로고    scopus 로고
    • The Gla domain of factor IXa binds to factor VIIIa in the tenase complex
    • Blostein M.D., Furie B.C., Rajotte I., Furie B. The Gla domain of factor IXa binds to factor VIIIa in the tenase complex. J Biol Chem 2003, 278:31297-31302.
    • (2003) J Biol Chem , vol.278 , pp. 31297-31302
    • Blostein, M.D.1    Furie, B.C.2    Rajotte, I.3    Furie, B.4
  • 24
    • 44449143420 scopus 로고    scopus 로고
    • Principles of assessing bacterial susceptibility to antibiotics using the agar diffusion method
    • Bonev B., Hooper J., Parisot J. Principles of assessing bacterial susceptibility to antibiotics using the agar diffusion method. Antimicrob Chemother 2008, 61:1295-1301.
    • (2008) Antimicrob Chemother , vol.61 , pp. 1295-1301
    • Bonev, B.1    Hooper, J.2    Parisot, J.3
  • 25
    • 79960345583 scopus 로고    scopus 로고
    • Structural determinants of the immunomodulatory properties of the C-terminal region of bovine β-casein
    • Bonomi F., Brandt R., Favalli S., Ferranti P., Fierro O., Frøkiær H., et al. Structural determinants of the immunomodulatory properties of the C-terminal region of bovine β-casein. Int Dairy J 2011, 21:770-776.
    • (2011) Int Dairy J , vol.21 , pp. 770-776
    • Bonomi, F.1    Brandt, R.2    Favalli, S.3    Ferranti, P.4    Fierro, O.5    Frøkiær, H.6
  • 26
    • 80054880017 scopus 로고    scopus 로고
    • High-value components and bioactives from sea cucumbers for functional foods - a review
    • Bordbar S., Anwar F., Saari N. High-value components and bioactives from sea cucumbers for functional foods - a review. Mar Drugs 2011, 9:1761-1805.
    • (2011) Mar Drugs , vol.9 , pp. 1761-1805
    • Bordbar, S.1    Anwar, F.2    Saari, N.3
  • 27
    • 60249083915 scopus 로고    scopus 로고
    • Antioxidant and free radical-scavenging activities of smooth hound (Mustelus mustelus) muscle protein hydrolysates obtained by gastrointestinal proteases
    • Bougatef A., Hajji M., Balti R., Lassoued I., Triki-Ellouz Y., Nasri M. Antioxidant and free radical-scavenging activities of smooth hound (Mustelus mustelus) muscle protein hydrolysates obtained by gastrointestinal proteases. Food Chem 2009, 114:1198-1205.
    • (2009) Food Chem , vol.114 , pp. 1198-1205
    • Bougatef, A.1    Hajji, M.2    Balti, R.3    Lassoued, I.4    Triki-Ellouz, Y.5    Nasri, M.6
  • 28
    • 69349093252 scopus 로고    scopus 로고
    • Purification and identification of novel antioxidant peptides from enzymatic hydrolysates of sardinelle (Sardinella aurita) by-products proteins
    • Bougatef A., Nedjar-Arroume N., Manni L., Ravallec R., Barkia A., Guillochon D., Nasri M. Purification and identification of novel antioxidant peptides from enzymatic hydrolysates of sardinelle (Sardinella aurita) by-products proteins. Food Chem 2010, 118(3):559-565.
    • (2010) Food Chem , vol.118 , Issue.3 , pp. 559-565
    • Bougatef, A.1    Nedjar-Arroume, N.2    Manni, L.3    Ravallec, R.4    Barkia, A.5    Guillochon, D.6    Nasri, M.7
  • 29
    • 21844525321 scopus 로고
    • Continuous hydrolysis of caseinomacropeptide in a membrane reactor: kinetic study and gram-scale production of antithrombotic peptides
    • Bouhallab S., Touzé C. Continuous hydrolysis of caseinomacropeptide in a membrane reactor: kinetic study and gram-scale production of antithrombotic peptides. Lait 1995, 75:251-258.
    • (1995) Lait , vol.75 , pp. 251-258
    • Bouhallab, S.1    Touzé, C.2
  • 30
    • 0000292524 scopus 로고
    • A note on the kinetics of enzyme action
    • Briggs G., Haldane J. A note on the kinetics of enzyme action. Biochem J 1925, 19:338-339.
    • (1925) Biochem J , vol.19 , pp. 338-339
    • Briggs, G.1    Haldane, J.2
  • 31
    • 0009212871 scopus 로고
    • Application of metabolic properties of lactic acid bacteria
    • Ardie Normandie, Caen, France, G. Novel, J.-F. Le Querler (Eds.)
    • Brink T.B., Huis In't Veld J.H.J. Application of metabolic properties of lactic acid bacteria. Les Bacteries Lactiques 1992, 67-76. Ardie Normandie, Caen, France. G. Novel, J.-F. Le Querler (Eds.).
    • (1992) Les Bacteries Lactiques , pp. 67-76
    • Brink, T.B.1    Huis In't Veld, J.H.J.2
  • 32
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: from invertebrates to vertebrates
    • Bulet P., Stocklin R., Menin L. Anti-microbial peptides: from invertebrates to vertebrates. Immunol Rev 2004, 198:169-184.
    • (2004) Immunol Rev , vol.198 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 33
    • 0034951098 scopus 로고    scopus 로고
    • Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin
    • Byun H.-G., Kim S.-K. Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin. Process Biochem 2001, 36:1155-1162.
    • (2001) Process Biochem , vol.36 , pp. 1155-1162
    • Byun, H.-G.1    Kim, S.-K.2
  • 34
    • 64949125943 scopus 로고    scopus 로고
    • Utilization of cross-linked laccase aggregates in a perfusion basket reactor for the continuous elimination of endocrine disrupting chemicals
    • Cabana H., Jones J.P., Agathos S.N. Utilization of cross-linked laccase aggregates in a perfusion basket reactor for the continuous elimination of endocrine disrupting chemicals. Biotechnol Bioeng 2009, 102:1582-1592.
    • (2009) Biotechnol Bioeng , vol.102 , pp. 1582-1592
    • Cabana, H.1    Jones, J.P.2    Agathos, S.N.3
  • 35
    • 0342804403 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of soy protein to improve its amino acid composition and functional properties
    • Calderón de la Barca A.M., Ruiz-Salazar R.A., Jara-Marini M.E. Enzymatic hydrolysis of soy protein to improve its amino acid composition and functional properties. J Food Sci 2000, 65:246-253.
    • (2000) J Food Sci , vol.65 , pp. 246-253
    • Calderón de la Barca, A.M.1    Ruiz-Salazar, R.A.2    Jara-Marini, M.E.3
  • 36
    • 78650713791 scopus 로고    scopus 로고
    • Angiotensin-I converting enzyme inhibitory and antioxidant activities of peptide fractions extracted by ultrafiltration of cowpea Vigna unguiculata hydrolysates
    • Campos M.R.S., Guerrero L.A.C., Ancona D.A.B. Angiotensin-I converting enzyme inhibitory and antioxidant activities of peptide fractions extracted by ultrafiltration of cowpea Vigna unguiculata hydrolysates. J Sci Food Agric 2010, 90:2512-2518.
    • (2010) J Sci Food Agric , vol.90 , pp. 2512-2518
    • Campos, M.R.S.1    Guerrero, L.A.C.2    Ancona, D.A.B.3
  • 37
    • 34548221362 scopus 로고    scopus 로고
    • Biocatalysis in non-conventional media - ionic liquids, supercritical fluids and the gas phase
    • Cantone S., Hanefeld U., Basso A. Biocatalysis in non-conventional media - ionic liquids, supercritical fluids and the gas phase. Green Chem 2007, 9:954-971.
    • (2007) Green Chem , vol.9 , pp. 954-971
    • Cantone, S.1    Hanefeld, U.2    Basso, A.3
  • 38
    • 77955576619 scopus 로고    scopus 로고
    • Purification and identification of an ACE inhibitory peptide from the peptic hydrolysate of Acetes chinensis and its antihypertensive effects in spontaneously hypertensive rats
    • Cao W., Zhang C., Hong P., Ji H., Hao J. Purification and identification of an ACE inhibitory peptide from the peptic hydrolysate of Acetes chinensis and its antihypertensive effects in spontaneously hypertensive rats. Int J Food Sci Technol 2010, 45:959-965.
    • (2010) Int J Food Sci Technol , vol.45 , pp. 959-965
    • Cao, W.1    Zhang, C.2    Hong, P.3    Ji, H.4    Hao, J.5
  • 39
    • 0041152088 scopus 로고    scopus 로고
    • Properties and synthetic applications of enzymes in organic solvents
    • Carrea G., Riva S. Properties and synthetic applications of enzymes in organic solvents. Angew Chem Int Ed 2000, 39:2226-2254.
    • (2000) Angew Chem Int Ed , vol.39 , pp. 2226-2254
    • Carrea, G.1    Riva, S.2
  • 40
    • 38749105097 scopus 로고    scopus 로고
    • Using Grote-Hynes theory to quantify dynamical effects on the reaction rate of enzymatic processes: the case of methyltransferases
    • Castillo R., Roca M., Soriano A., Moliner V., Tunon I. Using Grote-Hynes theory to quantify dynamical effects on the reaction rate of enzymatic processes: the case of methyltransferases. J Phys Chem 2008, B 112:529-534.
    • (2008) J Phys Chem , vol.B 112 , pp. 529-534
    • Castillo, R.1    Roca, M.2    Soriano, A.3    Moliner, V.4    Tunon, I.5
  • 42
    • 0030614844 scopus 로고    scopus 로고
    • Physiochemical and physiological mechanisms for the effects of food on drug absorption: the role of lipids and pH
    • Charman W.N., Porter C.J., Mithani S., Dressman J.B. Physiochemical and physiological mechanisms for the effects of food on drug absorption: the role of lipids and pH. J Pharm Sci 1997, 86:269-282.
    • (1997) J Pharm Sci , vol.86 , pp. 269-282
    • Charman, W.N.1    Porter, C.J.2    Mithani, S.3    Dressman, J.B.4
  • 43
    • 77049102128 scopus 로고    scopus 로고
    • Influence of temperature and degree of hydrolysis on the peptide composition of trypsin hydrolysates of β-lactoglobulin: Analysis by LC-ESI-TOF/MS
    • Cheison S.C., Schmitt M., Leeb E., Letzel T., Kulozik U. Influence of temperature and degree of hydrolysis on the peptide composition of trypsin hydrolysates of β-lactoglobulin: Analysis by LC-ESI-TOF/MS. Food Chem 2010, 121(2):457-467.
    • (2010) Food Chem , vol.121 , Issue.2 , pp. 457-467
    • Cheison, S.C.1    Schmitt, M.2    Leeb, E.3    Letzel, T.4    Kulozik, U.5
  • 44
    • 51749125645 scopus 로고    scopus 로고
    • Leaf protein's utilization status and its prospect
    • Chen W., Qiu Y. Leaf protein's utilization status and its prospect. Food Sci (Chin) 2003, 24:158-161.
    • (2003) Food Sci (Chin) , vol.24 , pp. 158-161
    • Chen, W.1    Qiu, Y.2
  • 45
    • 33751154733 scopus 로고
    • Structural analysis of antioxidative peptides from soybean β-conglycinin
    • Chen H.M., Muramoto K., Yamauchi F. Structural analysis of antioxidative peptides from soybean β-conglycinin. J Agric Food Chem 1995, 43:574-578.
    • (1995) J Agric Food Chem , vol.43 , pp. 574-578
    • Chen, H.M.1    Muramoto, K.2    Yamauchi, F.3
  • 46
    • 0028814173 scopus 로고
    • Isolation and characterization of immunostimulative peptides from soybean
    • Chen J.R., Suetsuna K., Yamauchi F. Isolation and characterization of immunostimulative peptides from soybean. J Nutr Biochem 1995, 6:310-313.
    • (1995) J Nutr Biochem , vol.6 , pp. 310-313
    • Chen, J.R.1    Suetsuna, K.2    Yamauchi, F.3
  • 47
    • 2542545209 scopus 로고    scopus 로고
    • Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein
    • Chen H.M., Muramoto K., Yamauchi F., Nokihara K. Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein. J Agric Food Chem 1996, 44:2619-2623.
    • (1996) J Agric Food Chem , vol.44 , pp. 2619-2623
    • Chen, H.M.1    Muramoto, K.2    Yamauchi, F.3    Nokihara, K.4
  • 48
    • 33847039492 scopus 로고    scopus 로고
    • Purification of angiotensin I-converting enzyme inhibitory peptides and antihypertensive effect of milk produced by protease facilitated lactic fermentation
    • Chen G.-W., Tsai J.-S., Pan B.-S. Purification of angiotensin I-converting enzyme inhibitory peptides and antihypertensive effect of milk produced by protease facilitated lactic fermentation. Int Dairy J 2007, 17:641-647.
    • (2007) Int Dairy J , vol.17 , pp. 641-647
    • Chen, G.-W.1    Tsai, J.-S.2    Pan, B.-S.3
  • 49
    • 71349084657 scopus 로고    scopus 로고
    • Antioxidant and emulsifying properties of potato protein hydrolysate in soybean oil-in-water emulsions
    • Cheng Y., Xiong Y.L., Chen J. Antioxidant and emulsifying properties of potato protein hydrolysate in soybean oil-in-water emulsions. Food Chem 2010, 120(1):101-108.
    • (2010) Food Chem , vol.120 , Issue.1 , pp. 101-108
    • Cheng, Y.1    Xiong, Y.L.2    Chen, J.3
  • 50
    • 0019332139 scopus 로고
    • Binding of peptide substrates and inhibitors of angiotensin-converting enzyme: importance of the COOH-terminal dipeptide sequence
    • Cheung H.-S., Wang F.-L., Ondetti M.A., Sabo E.F., Cushman D.W. Binding of peptide substrates and inhibitors of angiotensin-converting enzyme: importance of the COOH-terminal dipeptide sequence. J Biol Chem 1980, 255:401.
    • (1980) J Biol Chem , vol.255 , pp. 401
    • Cheung, H.-S.1    Wang, F.-L.2    Ondetti, M.A.3    Sabo, E.F.4    Cushman, D.W.5
  • 51
    • 79251543643 scopus 로고    scopus 로고
    • Selective internalization of selfassembled artificial oil bodies by HER2/neu-positive cells
    • 015102
    • Chiang C.J., Lin L.J., Lin C.C., Chang C.H., Chao Y.P. Selective internalization of selfassembled artificial oil bodies by HER2/neu-positive cells. Nanotechnology 2011, 015102.
    • (2011) Nanotechnology
    • Chiang, C.J.1    Lin, L.J.2    Lin, C.C.3    Chang, C.H.4    Chao, Y.P.5
  • 52
    • 4644251007 scopus 로고    scopus 로고
    • Hydrophobicity of bitter peptides from soy protein hydrolysates
    • Cho M.J., Unklesbay N., Hsieh F.H., Clarke A.D. Hydrophobicity of bitter peptides from soy protein hydrolysates. J Agric Food Chem 2004, 52:5895-5901.
    • (2004) J Agric Food Chem , vol.52 , pp. 5895-5901
    • Cho, M.J.1    Unklesbay, N.2    Hsieh, F.H.3    Clarke, A.D.4
  • 54
    • 84873730748 scopus 로고    scopus 로고
    • Potential applications of antioxidant compounds derived from algae
    • Chu W.L. Potential applications of antioxidant compounds derived from algae. Curr Topics Nutraceutical Res 2011, 9:83-98.
    • (2011) Curr Topics Nutraceutical Res , vol.9 , pp. 83-98
    • Chu, W.L.1
  • 55
    • 0037179121 scopus 로고    scopus 로고
    • Age-related decreases in Nurr1 immunoreactivity in the human substantia nigra
    • Chu Y., Kompoliti K., Cochran E.J., Mufson E.J., Kordower J.H. Age-related decreases in Nurr1 immunoreactivity in the human substantia nigra. J Comp Neurol 2002, 450:203-214.
    • (2002) J Comp Neurol , vol.450 , pp. 203-214
    • Chu, Y.1    Kompoliti, K.2    Cochran, E.J.3    Mufson, E.J.4    Kordower, J.H.5
  • 57
    • 0034199281 scopus 로고    scopus 로고
    • Bioactive milk peptides: a prospectus
    • Clare D.A., Swaisgood H.E. Bioactive milk peptides: a prospectus. J Dairy Sci 2000, 83:1187-1195.
    • (2000) J Dairy Sci , vol.83 , pp. 1187-1195
    • Clare, D.A.1    Swaisgood, H.E.2
  • 58
    • 76849088572 scopus 로고    scopus 로고
    • Identity of the immunomodulatory proteins from garlic (Allium sativum) with the major garlic lectins or agglutinins
    • Clement F., Pramod S.N., Venkatesh Y.P. Identity of the immunomodulatory proteins from garlic (Allium sativum) with the major garlic lectins or agglutinins. Int Immunopharmacol 2010, 10:316-324.
    • (2010) Int Immunopharmacol , vol.10 , pp. 316-324
    • Clement, F.1    Pramod, S.N.2    Venkatesh, Y.P.3
  • 59
    • 13844281684 scopus 로고    scopus 로고
    • Assays for oxidative stress and antioxidant status: applications to research into the biological effectiveness of polyphenols
    • Collins A.R. Assays for oxidative stress and antioxidant status: applications to research into the biological effectiveness of polyphenols. Am J Clin Nutr 2005, 81:261S-267S.
    • (2005) Am J Clin Nutr , vol.81 , pp. 261S-267S
    • Collins, A.R.1
  • 60
    • 79955549808 scopus 로고    scopus 로고
    • Food-grade production of an antihypertensive casein hydrolysate and resistance of active peptides to drying and storage
    • Contreras M.M., Sevilla M.A., Monroy-Ruiz J., Amigo L., Gómez-Sala B., Molina E., et al. Food-grade production of an antihypertensive casein hydrolysate and resistance of active peptides to drying and storage. Int Dairy J 2011, 21(7):470-476.
    • (2011) Int Dairy J , vol.21 , Issue.7 , pp. 470-476
    • Contreras, M.M.1    Sevilla, M.A.2    Monroy-Ruiz, J.3    Amigo, L.4    Gómez-Sala, B.5    Molina, E.6
  • 61
    • 0026652726 scopus 로고
    • Identification of C-terminal peptides of bovine β-casein that enhance proliferation of rat lymphocytes
    • Coste M., Rochet V., Leonil J., Molle D., Bouhallab S., Tomé D. Identification of C-terminal peptides of bovine β-casein that enhance proliferation of rat lymphocytes. Immunol Lett 1992, 33:41-46.
    • (1992) Immunol Lett , vol.33 , pp. 41-46
    • Coste, M.1    Rochet, V.2    Leonil, J.3    Molle, D.4    Bouhallab, S.5    Tomé, D.6
  • 62
    • 80051793850 scopus 로고    scopus 로고
    • Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization
    • Cowan D.A., Lafuente R.F. Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization. Enzyme Microb Technol 2011, 49:326-346.
    • (2011) Enzyme Microb Technol , vol.49 , pp. 326-346
    • Cowan, D.A.1    Lafuente, R.F.2
  • 63
    • 17644386230 scopus 로고    scopus 로고
    • Physicochemical characterization of casein phosphopeptideamorphous calcium phosphate nanocomplexes
    • Cross K.J., Huq N.L., Palamara J.E., Perich J.W., Reynolds E.C. Physicochemical characterization of casein phosphopeptideamorphous calcium phosphate nanocomplexes. J Biol Chem 2005, 280:15362-15369.
    • (2005) J Biol Chem , vol.280 , pp. 15362-15369
    • Cross, K.J.1    Huq, N.L.2    Palamara, J.E.3    Perich, J.W.4    Reynolds, E.C.5
  • 64
    • 0027909093 scopus 로고
    • Dramatic enhancement of enzymatic activity in organic solvents by lyoprotectants
    • Dabulis K., Klibanov A.M. Dramatic enhancement of enzymatic activity in organic solvents by lyoprotectants. Biotechnol Bioeng 1993, 41:566-571.
    • (1993) Biotechnol Bioeng , vol.41 , pp. 566-571
    • Dabulis, K.1    Klibanov, A.M.2
  • 65
    • 4444238114 scopus 로고    scopus 로고
    • Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis
    • Davalos A., Miguel M., Bartolome B., Lopez-Fandino R. Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis. J Food Prot 2004, 67:1939-1944.
    • (2004) J Food Prot , vol.67 , pp. 1939-1944
    • Davalos, A.1    Miguel, M.2    Bartolome, B.3    Lopez-Fandino, R.4
  • 66
    • 36349012420 scopus 로고    scopus 로고
    • Intrinsic pathway of coagulation and arterial thrombosis
    • David G., Thomas R. Intrinsic pathway of coagulation and arterial thrombosis. Arterioscler Thromb Vasc Biol 2007, 27:2507-2513.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 2507-2513
    • David, G.1    Thomas, R.2
  • 67
    • 0037124546 scopus 로고    scopus 로고
    • The origin of pegnology
    • Davis F. The origin of pegnology. Adv Drug Deliv Rev 2002, 54:457-458.
    • (2002) Adv Drug Deliv Rev , vol.54 , pp. 457-458
    • Davis, F.1
  • 68
    • 0033491620 scopus 로고    scopus 로고
    • The controlled introduction of multiple negative charges at single amino acid sites in subtilisin Bacillus lentus
    • Davis B.G., Shang X., DeSantis G., Bott R.R., Jones J.B. The controlled introduction of multiple negative charges at single amino acid sites in subtilisin Bacillus lentus. Bioorg Med Chem 1999, 7:2293-2301.
    • (1999) Bioorg Med Chem , vol.7 , pp. 2293-2301
    • Davis, B.G.1    Shang, X.2    DeSantis, G.3    Bott, R.R.4    Jones, J.B.5
  • 69
    • 0021501694 scopus 로고
    • Factors regulating the exchange of nutrients and drugs between lymph and blood in the small intestine
    • Deak S.T., Csáky T.Z. Factors regulating the exchange of nutrients and drugs between lymph and blood in the small intestine. Microcirc Endothel Lymphat 1984, 1:569-588.
    • (1984) Microcirc Endothel Lymphat , vol.1 , pp. 569-588
    • Deak, S.T.1    Csáky, T.Z.2
  • 70
    • 11144231660 scopus 로고    scopus 로고
    • Antioxidant mechanisms of caseinophosphopeptides and casein hydrolysates and their application in ground beef
    • Diaz M., Decker E.A. Antioxidant mechanisms of caseinophosphopeptides and casein hydrolysates and their application in ground beef. J Agric Food Chem 2005, 52:8208-8213.
    • (2005) J Agric Food Chem , vol.52 , pp. 8208-8213
    • Diaz, M.1    Decker, E.A.2
  • 71
    • 0026731584 scopus 로고
    • Synthesis of a homologous series of ketomethyl arginyl pseudodipeptides and application to low molecular weight hirudin-like thrombin inhibitors
    • DiMaio J., Gibbs B.F., Lefebvre J., Munn D. Synthesis of a homologous series of ketomethyl arginyl pseudodipeptides and application to low molecular weight hirudin-like thrombin inhibitors. J Med Chem 1992, 35:3331-3341.
    • (1992) J Med Chem , vol.35 , pp. 3331-3341
    • DiMaio, J.1    Gibbs, B.F.2    Lefebvre, J.3    Munn, D.4
  • 72
    • 79958843995 scopus 로고    scopus 로고
    • Associations between dairy consumption and body weight: a review of the evidence and underlying mechanisms
    • Dougkas A., Reynolds C.K., Givens I.D., Elwood P.C., Minihane A.M. Associations between dairy consumption and body weight: a review of the evidence and underlying mechanisms. Nutr Res Rev 2011, 24:72-95.
    • (2011) Nutr Res Rev , vol.24 , pp. 72-95
    • Dougkas, A.1    Reynolds, C.K.2    Givens, I.D.3    Elwood, P.C.4    Minihane, A.M.5
  • 73
    • 84858707910 scopus 로고    scopus 로고
    • Discovery of bioactive compounds from marine fungi: current analytical techniques and future perspectives
    • Duarte K., Rocha-Santos T.A.P., Freitas A.C., Duarte A.C. Discovery of bioactive compounds from marine fungi: current analytical techniques and future perspectives. Trends Anal Chem 2012, 34:97-110.
    • (2012) Trends Anal Chem , vol.34 , pp. 97-110
    • Duarte, K.1    Rocha-Santos, T.A.P.2    Freitas, A.C.3    Duarte, A.C.4
  • 75
    • 33947716554 scopus 로고    scopus 로고
    • Ionic liquids as a medium for enantioselective catalysis
    • Durand J., Teuma E., Gómez M. Ionic liquids as a medium for enantioselective catalysis. C R Chim 2007, 10:152-177.
    • (2007) C R Chim , vol.10 , pp. 152-177
    • Durand, J.1    Teuma, E.2    Gómez, M.3
  • 78
    • 42149124475 scopus 로고    scopus 로고
    • Anthocyanins inhibit peroxyl radical-induced apoptosis in Caco-2 cells
    • Elisia I., Kitts D.D. Anthocyanins inhibit peroxyl radical-induced apoptosis in Caco-2 cells. Mol Cell Biochem 2008, 312:139-145.
    • (2008) Mol Cell Biochem , vol.312 , pp. 139-145
    • Elisia, I.1    Kitts, D.D.2
  • 79
    • 84855813140 scopus 로고    scopus 로고
    • Albumin-based nanoparticles as potential controlled release drug delivery systems
    • Elzoghby A.O., Samy W.M., Elgindy N.A. Albumin-based nanoparticles as potential controlled release drug delivery systems. J Control Release 2012, 157:168-182.
    • (2012) J Control Release , vol.157 , pp. 168-182
    • Elzoghby, A.O.1    Samy, W.M.2    Elgindy, N.A.3
  • 80
    • 51049097278 scopus 로고    scopus 로고
    • The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease
    • Erdmann K., Cheung B.W.Y., Schröder H. The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. J Nutr Biol 2008, 19:643-654.
    • (2008) J Nutr Biol , vol.19 , pp. 643-654
    • Erdmann, K.1    Cheung, B.W.Y.2    Schröder, H.3
  • 81
    • 51249120487 scopus 로고    scopus 로고
    • Effect of milk proteins and their hydrolysates on in vitro immune responses
    • Eriksen E.K., Vegarud G.E., Langsrud T., Almaas H., Lea T. Effect of milk proteins and their hydrolysates on in vitro immune responses. Small Rumin Res 2008, 79:29-37.
    • (2008) Small Rumin Res , vol.79 , pp. 29-37
    • Eriksen, E.K.1    Vegarud, G.E.2    Langsrud, T.3    Almaas, H.4    Lea, T.5
  • 82
    • 0036113725 scopus 로고    scopus 로고
    • X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation
    • Estevez M., Skarda J., Spencer J., Banaszak L., Weaver T.M. X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation. Prot Sci 2002, 11:1552-1557.
    • (2002) Prot Sci , vol.11 , pp. 1552-1557
    • Estevez, M.1    Skarda, J.2    Spencer, J.3    Banaszak, L.4    Weaver, T.M.5
  • 83
    • 2542580915 scopus 로고    scopus 로고
    • Production of angiotensin I converting enzyme inhibitory peptides from sea bream scales
    • Fahmi A., Morimura S., Guo H.C., Shigematsu T., Kida K., Uemura Y. Production of angiotensin I converting enzyme inhibitory peptides from sea bream scales. Process Biochem 2004, 39:1195-1200.
    • (2004) Process Biochem , vol.39 , pp. 1195-1200
    • Fahmi, A.1    Morimura, S.2    Guo, H.C.3    Shigematsu, T.4    Kida, K.5    Uemura, Y.6
  • 84
    • 34249088582 scopus 로고    scopus 로고
    • Purification and characterization of an immunomodulatory peptide from bovine placenta water-soluble extract
    • Fang X.-P., Xia W.-S., Sheng Q.-H., Wang Y.-L. Purification and characterization of an immunomodulatory peptide from bovine placenta water-soluble extract. Prep Biochem Biotechnol 2007, 37:173-184.
    • (2007) Prep Biochem Biotechnol , vol.37 , pp. 173-184
    • Fang, X.-P.1    Xia, W.-S.2    Sheng, Q.-H.3    Wang, Y.-L.4
  • 85
    • 77954957021 scopus 로고    scopus 로고
    • Antioxidant activity of yoghurt peptides: Part 1-in vitro assays and evaluation in ω-3 enriched milk
    • Farvin K.H.S., Baron C.P., Nielsen N.S., Jacobsen C. Antioxidant activity of yoghurt peptides: Part 1-in vitro assays and evaluation in ω-3 enriched milk. Food Chem 2010, 123:1081-1089.
    • (2010) Food Chem , vol.123 , pp. 1081-1089
    • Farvin, K.H.S.1    Baron, C.P.2    Nielsen, N.S.3    Jacobsen, C.4
  • 86
    • 77954953719 scopus 로고    scopus 로고
    • Antioxidant activity of yoghurt peptides: Part 2 - Characterisation of peptide fractions
    • Farvin K.H.S., Baron C.P., Nielsen N.S., Otte J., Jacobsen C. Antioxidant activity of yoghurt peptides: Part 2 - Characterisation of peptide fractions. Food Chem 2010, 123:1090-1097.
    • (2010) Food Chem , vol.123 , pp. 1090-1097
    • Farvin, K.H.S.1    Baron, C.P.2    Nielsen, N.S.3    Otte, J.4    Jacobsen, C.5
  • 87
    • 33845983267 scopus 로고    scopus 로고
    • Preparation of ingredients containing an ACE-inhibitory peptide by tryptic hydrolysis of whey protein concentrates
    • Ferreira I.M.P.L.V.O., Pinho O., Mota M.V., Tavares P., Pereira A., Gonc-alves M.P., et al. Preparation of ingredients containing an ACE-inhibitory peptide by tryptic hydrolysis of whey protein concentrates. Int Dairy J 2007, 17:481-487.
    • (2007) Int Dairy J , vol.17 , pp. 481-487
    • Ferreira, I.M.P.L.V.O.1    Pinho, O.2    Mota, M.V.3    Tavares, P.4    Pereira, A.5    Gonc-alves, M.P.6
  • 88
    • 0024345057 scopus 로고
    • Biologically active peptides of casein and lactotransferrin implicated in platelet function
    • Fiat A.M., Levy-Toledano S., Caen J.P., Jollés P. Biologically active peptides of casein and lactotransferrin implicated in platelet function. J Dairy Res 1989, 56:351-355.
    • (1989) J Dairy Res , vol.56 , pp. 351-355
    • Fiat, A.M.1    Levy-Toledano, S.2    Caen, J.P.3    Jollés, P.4
  • 89
    • 0034492049 scopus 로고    scopus 로고
    • Milk protein-derived peptide inhibitors of angiotensin-I-converting enzyme
    • FitzGerald R.J., Meisel H. Milk protein-derived peptide inhibitors of angiotensin-I-converting enzyme. Br J Nutr 2000, 84:S33-S37.
    • (2000) Br J Nutr , vol.84 , pp. S33-S37
    • FitzGerald, R.J.1    Meisel, H.2
  • 90
    • 33645983664 scopus 로고    scopus 로고
    • Bioactive peptides and lactic fermentations
    • Fitzgerald R.J., Murray B.A. Bioactive peptides and lactic fermentations. Int J Dairy Technol 2006, 59:118-125.
    • (2006) Int J Dairy Technol , vol.59 , pp. 118-125
    • Fitzgerald, R.J.1    Murray, B.A.2
  • 91
    • 1842478225 scopus 로고    scopus 로고
    • Hypotensive peptides from milk proteins
    • Fitzgerald R.J., Murray B.A., Walsh D.J. Hypotensive peptides from milk proteins. J Nutr 2004, 134:980S.
    • (2004) J Nutr , vol.134 , pp. 980S
    • Fitzgerald, R.J.1    Murray, B.A.2    Walsh, D.J.3
  • 92
    • 69749111280 scopus 로고    scopus 로고
    • Modeling of the relationship between dipeptide structure and dipeptide stability, permeability, and ACE inhibitory activity
    • Foltz M., Buren L.V., Klaffke W., Duchateau G.S.M.J.E. Modeling of the relationship between dipeptide structure and dipeptide stability, permeability, and ACE inhibitory activity. J Food Sci 2009, 74(7):243-251.
    • (2009) J Food Sci , vol.74 , Issue.7 , pp. 243-251
    • Foltz, M.1    Buren, L.V.2    Klaffke, W.3    Duchateau, G.S.M.J.E.4
  • 93
    • 0032760778 scopus 로고    scopus 로고
    • A prodrug-type ACE-inhibitory peptide derived from fish protein
    • Fujita H., Yoshikawa M.L.K.P.N.M. A prodrug-type ACE-inhibitory peptide derived from fish protein. Immunopharmacology 1999, 44:123-127.
    • (1999) Immunopharmacology , vol.44 , pp. 123-127
    • Fujita, H.1    Yoshikawa, M.L.K.P.N.M.2
  • 94
    • 0033860508 scopus 로고    scopus 로고
    • Classification and antihypertensive activity of Angiotensin I-converting enzyme inhibitory peptides derived from food proteins
    • Fujita H., Yokoyama K., Yoshikawa M. Classification and antihypertensive activity of Angiotensin I-converting enzyme inhibitory peptides derived from food proteins. J Food Sci 2000, 65(4):564-569.
    • (2000) J Food Sci , vol.65 , Issue.4 , pp. 564-569
    • Fujita, H.1    Yokoyama, K.2    Yoshikawa, M.3
  • 95
    • 0002260166 scopus 로고    scopus 로고
    • Protein digestion and assimilation
    • Lippincott Williams and Wilkins, Philadelphia, PA, T. Yamada (Ed.)
    • Ganapathy V., Leibach F.H. Protein digestion and assimilation. Textbook of gastroenterology 1999, 456-467. Lippincott Williams and Wilkins, Philadelphia, PA. T. Yamada (Ed.).
    • (1999) Textbook of gastroenterology , pp. 456-467
    • Ganapathy, V.1    Leibach, F.H.2
  • 96
    • 0034883262 scopus 로고    scopus 로고
    • Transport characteristics of peptides and peptidomimetics: I. N-methylated peptides as substrates for the oligopeptide transporter and P-glycoprotein in the intestinal mucosa
    • Gao J., Sudoh M., Aubé J., Borchardt R.T. Transport characteristics of peptides and peptidomimetics: I. N-methylated peptides as substrates for the oligopeptide transporter and P-glycoprotein in the intestinal mucosa. J Pept Res 2001, 57:316-329.
    • (2001) J Pept Res , vol.57 , pp. 316-329
    • Gao, J.1    Sudoh, M.2    Aubé, J.3    Borchardt, R.T.4
  • 98
    • 0346726109 scopus 로고    scopus 로고
    • How enzymes work: analysis by modern rate theory and computer simulations
    • García-Viloca M., Gao J., Karplus M., Truhlar D.G. How enzymes work: analysis by modern rate theory and computer simulations. Science 2004, 303:186-195.
    • (2004) Science , vol.303 , pp. 186-195
    • García-Viloca, M.1    Gao, J.2    Karplus, M.3    Truhlar, D.G.4
  • 99
    • 0021475428 scopus 로고
    • Intestinal assimilation of intact peptides and proteins from the diet - a neglected field?
    • Gardner M.L.G. Intestinal assimilation of intact peptides and proteins from the diet - a neglected field?. Biol Rev 1984, 59:289-331.
    • (1984) Biol Rev , vol.59 , pp. 289-331
    • Gardner, M.L.G.1
  • 100
    • 0024147740 scopus 로고
    • Gastrointestinal absorption of intact proteins
    • Gardner M.L.G. Gastrointestinal absorption of intact proteins. Annu Rev Nutr 1988, 8:329-350.
    • (1988) Annu Rev Nutr , vol.8 , pp. 329-350
    • Gardner, M.L.G.1
  • 101
    • 33748312144 scopus 로고    scopus 로고
    • Immunomodulatory peptides obtained by the enzymatic hydrolysis of whey proteins
    • Gauthier S.F., Pouliot Y., Saint-Sauveur D. Immunomodulatory peptides obtained by the enzymatic hydrolysis of whey proteins. Int Dairy J 2006, 16(11):1315-1323.
    • (2006) Int Dairy J , vol.16 , Issue.11 , pp. 1315-1323
    • Gauthier, S.F.1    Pouliot, Y.2    Saint-Sauveur, D.3
  • 102
    • 80051797411 scopus 로고    scopus 로고
    • Purification and identification of ACE inhibitory peptides from Haruan (Channa striatus) myofibrillar protein hydrolysate using HPLC-ESI-TOF MS/MS
    • Ghassem M., Arihara K., Babji A.S., Said M., Ibrahim S. Purification and identification of ACE inhibitory peptides from Haruan (Channa striatus) myofibrillar protein hydrolysate using HPLC-ESI-TOF MS/MS. Food Chem 2011, 129(4):1770-1777.
    • (2011) Food Chem , vol.129 , Issue.4 , pp. 1770-1777
    • Ghassem, M.1    Arihara, K.2    Babji, A.S.3    Said, M.4    Ibrahim, S.5
  • 103
    • 1242300061 scopus 로고    scopus 로고
    • Production and characterization of bioactive peptides from soy hydrolysate and soy-fermented food
    • Gibbs B.F., Zougman A., Masse R., Mulligan C. Production and characterization of bioactive peptides from soy hydrolysate and soy-fermented food. Food Res Int 2004, 37:123-131.
    • (2004) Food Res Int , vol.37 , pp. 123-131
    • Gibbs, B.F.1    Zougman, A.2    Masse, R.3    Mulligan, C.4
  • 104
  • 105
    • 77953915015 scopus 로고    scopus 로고
    • Effect of chickpea protein hydrolysates on cell proliferation and in vitro bioavailability
    • Girón-Calle J., Alaiz M., Vioque J. Effect of chickpea protein hydrolysates on cell proliferation and in vitro bioavailability. Food Res Int 2010, 43:1365-1370.
    • (2010) Food Res Int , vol.43 , pp. 1365-1370
    • Girón-Calle, J.1    Alaiz, M.2    Vioque, J.3
  • 106
    • 0036380805 scopus 로고    scopus 로고
    • Angiotensin converting enzyme-inhibitory peptides in Manchego cheeses manufactured with different starter cultures
    • Gómez-Ruiz J.A., Ramos M., Recio I. Angiotensin converting enzyme-inhibitory peptides in Manchego cheeses manufactured with different starter cultures. Int Dairy J 2002, 12:697-706.
    • (2002) Int Dairy J , vol.12 , pp. 697-706
    • Gómez-Ruiz, J.A.1    Ramos, M.2    Recio, I.3
  • 107
    • 4744361004 scopus 로고    scopus 로고
    • ACE-inhibitory activity and structural properties of peptide Asp-Lys-Ile-His-Pro [beta-CN f(47-51)]. Study of the peptide forms synthesized by different methods
    • Gómez-Ruiz J.A., Recio I., Belloque J. ACE-inhibitory activity and structural properties of peptide Asp-Lys-Ile-His-Pro [beta-CN f(47-51)]. Study of the peptide forms synthesized by different methods. J Agric Food Chem 2004, 52(20):6315-6319.
    • (2004) J Agric Food Chem , vol.52 , Issue.20 , pp. 6315-6319
    • Gómez-Ruiz, J.A.1    Recio, I.2    Belloque, J.3
  • 110
    • 0028128349 scopus 로고
    • The significance of peptides in clinical nutrition
    • Grimble G.K. The significance of peptides in clinical nutrition. Annu Rev Nutr 1994, 14:419-447.
    • (1994) Annu Rev Nutr , vol.14 , pp. 419-447
    • Grimble, G.K.1
  • 111
    • 0034570845 scopus 로고    scopus 로고
    • Mechanisms of peptide and amino acid transport and their regulation
    • Nestec Ltd., Basel, P. Fürst, V. Young (Eds.) Proteins, peptides and amino acids
    • Grimble G.K. Mechanisms of peptide and amino acid transport and their regulation. Enteral Nutrition 2000, 63-88. Nestec Ltd., Basel. P. Fürst, V. Young (Eds.).
    • (2000) Enteral Nutrition , pp. 63-88
    • Grimble, G.K.1
  • 112
    • 0025636491 scopus 로고
    • A highly active and oxidation resistant subtilisin-like enzyme produced by a combination of site-directed mutagenesis and chemical modification
    • Gron H., Bech L.M., Branner S., Breddam K. A highly active and oxidation resistant subtilisin-like enzyme produced by a combination of site-directed mutagenesis and chemical modification. Eur J Biochem 1990, 194:897-901.
    • (1990) Eur J Biochem , vol.194 , pp. 897-901
    • Gron, H.1    Bech, L.M.2    Branner, S.3    Breddam, K.4
  • 113
    • 77952534146 scopus 로고    scopus 로고
    • Rapid emergence of multimarker strategies in laboratory medicine
    • Gruson D., Bodovitz S. Rapid emergence of multimarker strategies in laboratory medicine. Biomarker 2010, 15:289-296.
    • (2010) Biomarker , vol.15 , pp. 289-296
    • Gruson, D.1    Bodovitz, S.2
  • 114
    • 58249134379 scopus 로고    scopus 로고
    • Optimisation of hydrolysis conditions for the production of the angiotensin-I converting enzyme (ACE) inhibitory peptides from whey protein using response surface methodology
    • Guo Y., Pan D., Tanokura M. Optimisation of hydrolysis conditions for the production of the angiotensin-I converting enzyme (ACE) inhibitory peptides from whey protein using response surface methodology. Food Chem 2009, 114:328-333.
    • (2009) Food Chem , vol.114 , pp. 328-333
    • Guo, Y.1    Pan, D.2    Tanokura, M.3
  • 115
    • 33749322995 scopus 로고    scopus 로고
    • Peptide fractions of rapeseed hydrolysates as an alternative to animal proteins in CHO cell culture media
    • Haddani B.F., Tessier B., Chenu S., Chevalot I., Harscoat C., Marc I., et al. Peptide fractions of rapeseed hydrolysates as an alternative to animal proteins in CHO cell culture media. Process Biochem 2006, 41:2297-2304.
    • (2006) Process Biochem , vol.41 , pp. 2297-2304
    • Haddani, B.F.1    Tessier, B.2    Chenu, S.3    Chevalot, I.4    Harscoat, C.5    Marc, I.6
  • 116
    • 0033174892 scopus 로고    scopus 로고
    • Purification and identification of potentially bioactive peptides from enzyme-modified cheese
    • Haileselassie S.S., Lee B.H., Gibbs B.F. Purification and identification of potentially bioactive peptides from enzyme-modified cheese. J Dairy Sci 1999, 82:1612-1617.
    • (1999) J Dairy Sci , vol.82 , pp. 1612-1617
    • Haileselassie, S.S.1    Lee, B.H.2    Gibbs, B.F.3
  • 117
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and hostdefense peptides as new anti-infective therapeutic strategies
    • Hancock R.E.W., Sahl H.-G. Antimicrobial and hostdefense peptides as new anti-infective therapeutic strategies. Nat Biotechnol 2006, 24(12):1551-1557.
    • (2006) Nat Biotechnol , vol.24 , Issue.12 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.-G.2
  • 118
    • 34147123803 scopus 로고    scopus 로고
    • Food-derived peptides with biological activity: from research to food applications
    • Hartmann R., Meisel H. Food-derived peptides with biological activity: from research to food applications. Curr Opin Biotechnol 2007, 18:163-169.
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 163-169
    • Hartmann, R.1    Meisel, H.2
  • 119
    • 0027453181 scopus 로고
    • Purification of cysteine-rich bioactive peptides from leukocytes by continuous acid-urea-polyacrylamide gel electrophoresis
    • Harwig S.S.L., Chen N.P., Park A.S.K., Lehrer R.I. Purification of cysteine-rich bioactive peptides from leukocytes by continuous acid-urea-polyacrylamide gel electrophoresis. Anal Biochem 1993, 208:382-386.
    • (1993) Anal Biochem , vol.208 , pp. 382-386
    • Harwig, S.S.L.1    Chen, N.P.2    Park, A.S.K.3    Lehrer, R.I.4
  • 120
    • 78650190377 scopus 로고    scopus 로고
    • Characterisation of fibre-rich powder and antioxidant capacity of Mangifera pajang K. fruit peels
    • Hassan F.A., Ismail A., Abdul-Hamid A., Azlan A., Al-sheraji S.H. Characterisation of fibre-rich powder and antioxidant capacity of Mangifera pajang K. fruit peels. Food Chem 2011, 126:283-288.
    • (2011) Food Chem , vol.126 , pp. 283-288
    • Hassan, F.A.1    Ismail, A.2    Abdul-Hamid, A.3    Azlan, A.4    Al-sheraji, S.H.5
  • 121
    • 65549122580 scopus 로고    scopus 로고
    • Isolation and identification of antihypertensive peptides from antarctic krill tail meat hydrolysate
    • Hatanaka A., Miyahara H., Suzuki K.I., Sato S. Isolation and identification of antihypertensive peptides from antarctic krill tail meat hydrolysate. J Food Sci 2009, 74(4):116-120.
    • (2009) J Food Sci , vol.74 , Issue.4 , pp. 116-120
    • Hatanaka, A.1    Miyahara, H.2    Suzuki, K.I.3    Sato, S.4
  • 122
    • 78650818528 scopus 로고    scopus 로고
    • Control of protein immobilization. Coupling immobilization and site directed mutagenesis to improve biocatalyst or biosensor performance
    • Hernandez K., Fernandez-Lafuente R. Control of protein immobilization. Coupling immobilization and site directed mutagenesis to improve biocatalyst or biosensor performance. Enzyme Microb Technol 2011, 48:107-122.
    • (2011) Enzyme Microb Technol , vol.48 , pp. 107-122
    • Hernandez, K.1    Fernandez-Lafuente, R.2
  • 124
    • 35348827743 scopus 로고    scopus 로고
    • Effect of simulated gastrointestinal digestion on the antihypertensive properties of synthetic beta-lactoglobulin peptide sequences
    • Hernández-Ledesma B., Miguel M., Amigo L., Aleixandre M.A., Recio I. Effect of simulated gastrointestinal digestion on the antihypertensive properties of synthetic beta-lactoglobulin peptide sequences. J Dairy Res 2007, 74:336.
    • (2007) J Dairy Res , vol.74 , pp. 336
    • Hernández-Ledesma, B.1    Miguel, M.2    Amigo, L.3    Aleixandre, M.A.4    Recio, I.5
  • 125
    • 0037350641 scopus 로고    scopus 로고
    • Production of enterolysin A by a raw milk enterococcal isolate exhibiting multiple virulence factors
    • Hickey R.M., Twomey D.P., Ross R.P., Hill C. Production of enterolysin A by a raw milk enterococcal isolate exhibiting multiple virulence factors. Microbiology 2003, 149:655-664.
    • (2003) Microbiology , vol.149 , pp. 655-664
    • Hickey, R.M.1    Twomey, D.P.2    Ross, R.P.3    Hill, C.4
  • 126
    • 0020956616 scopus 로고
    • Multiple endogenous opioid peptide
    • Hollt V. Multiple endogenous opioid peptide. Trends Neurosci 1983, 6:24-26.
    • (1983) Trends Neurosci , vol.6 , pp. 24-26
    • Hollt, V.1
  • 127
    • 0034811591 scopus 로고    scopus 로고
    • Proteolysis of ProPTHrP(1-141) by "prohormone thiol protease" at multibasic residues generates PTHrP-related peptides: implications for PTHrP peptide production in lung cancer cells
    • Hook V.Y.H., Burton D., Yasothornsrikul S., Hastings R.H., Deftos L.J. Proteolysis of ProPTHrP(1-141) by "prohormone thiol protease" at multibasic residues generates PTHrP-related peptides: implications for PTHrP peptide production in lung cancer cells. Biochem Biophys Res Commun 2001, 285:932-938.
    • (2001) Biochem Biophys Res Commun , vol.285 , pp. 932-938
    • Hook, V.Y.H.1    Burton, D.2    Yasothornsrikul, S.3    Hastings, R.H.4    Deftos, L.J.5
  • 128
    • 29344463656 scopus 로고    scopus 로고
    • Effect of wheat gluten hydrolysate on the immune system in healthy human subjects
    • Horiguchi N., Horiguchi H., Suzuki Y. Effect of wheat gluten hydrolysate on the immune system in healthy human subjects. Biosci Biotechnol Biochem 2005, 69:2445-2449.
    • (2005) Biosci Biotechnol Biochem , vol.69 , pp. 2445-2449
    • Horiguchi, N.1    Horiguchi, H.2    Suzuki, Y.3
  • 129
    • 84862813217 scopus 로고    scopus 로고
    • Purification and identification of immunomodulating peptides from enzymatic hydrolysates of Alaska pollock frame
    • Hou H., Fan Y., Li B., Xue C., Yu G., Zhang Z., et al. Purification and identification of immunomodulating peptides from enzymatic hydrolysates of Alaska pollock frame. Food Chem 2012, 134:821-828.
    • (2012) Food Chem , vol.134 , pp. 821-828
    • Hou, H.1    Fan, Y.2    Li, B.3    Xue, C.4    Yu, G.5    Zhang, Z.6
  • 130
    • 67349098428 scopus 로고    scopus 로고
    • Antioxidative properties of peptides prepared from tuna cooking juice hydrolysates with orientase (Bacillus subtilis)
    • Hsu K.-C., Lu G.-H., Jao C.-L. Antioxidative properties of peptides prepared from tuna cooking juice hydrolysates with orientase (Bacillus subtilis). Food Res Int 2009, 42(5-6):647-652.
    • (2009) Food Res Int , vol.42 , Issue.5-6 , pp. 647-652
    • Hsu, K.-C.1    Lu, G.-H.2    Jao, C.-L.3
  • 131
    • 77950595188 scopus 로고    scopus 로고
    • Purification of antioxidative peptides prepared from enzymatic hydrolysates of tuna dark muscle by-product
    • Hsu K.C. Purification of antioxidative peptides prepared from enzymatic hydrolysates of tuna dark muscle by-product. Food Chem 2010, 122(1):42-48.
    • (2010) Food Chem , vol.122 , Issue.1 , pp. 42-48
    • Hsu, K.C.1
  • 132
    • 77954620023 scopus 로고    scopus 로고
    • Oxygen radical absorbance capacity of peptides from egg white protein ovotransferrin and their interaction phytochemicals
    • Huang W.Y., Majumder K., Wu J. Oxygen radical absorbance capacity of peptides from egg white protein ovotransferrin and their interaction phytochemicals. Food Chem 2010, 123(3):635-641.
    • (2010) Food Chem , vol.123 , Issue.3 , pp. 635-641
    • Huang, W.Y.1    Majumder, K.2    Wu, J.3
  • 133
    • 79958038487 scopus 로고    scopus 로고
    • Antihypertensive effect of corn peptides, produced by a continuous production in enzymatic membrane reactor, in spontaneously hypertensive rats
    • Huang W.-H., Sun J., He H., Dong H.-W., Li J.-T. Antihypertensive effect of corn peptides, produced by a continuous production in enzymatic membrane reactor, in spontaneously hypertensive rats. Food Chem 2011, 128:968-973.
    • (2011) Food Chem , vol.128 , pp. 968-973
    • Huang, W.-H.1    Sun, J.2    He, H.3    Dong, H.-W.4    Li, J.-T.5
  • 134
    • 33745281704 scopus 로고    scopus 로고
    • Protective effect of Centella asiatica extract and powder on oxidative stress in rats
    • Hussin M., Abdul-Hamid A., Mohamad S., Saari N., Ismail M., Bejo M.H. Protective effect of Centella asiatica extract and powder on oxidative stress in rats. Food Chem 2007, 100:535-541.
    • (2007) Food Chem , vol.100 , pp. 535-541
    • Hussin, M.1    Abdul-Hamid, A.2    Mohamad, S.3    Saari, N.4    Ismail, M.5    Bejo, M.H.6
  • 135
    • 84903421873 scopus 로고    scopus 로고
    • Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin
    • Hwang P.M., Zhou N., Shan X., Arrowsmith C.H., Vogel H.J. Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry 1998, 37(12):4288-4298.
    • (1998) Biochemistry , vol.37 , Issue.12 , pp. 4288-4298
    • Hwang, P.M.1    Zhou, N.2    Shan, X.3    Arrowsmith, C.H.4    Vogel, H.J.5
  • 136
    • 34249715284 scopus 로고    scopus 로고
    • Major hemorrhage and tolerability of warfarin in the first year of therapy among elderly patients with atrial fibrillation
    • Hylek E.M., Molina C.E., Shea C., Henault L.E., Regan S. Major hemorrhage and tolerability of warfarin in the first year of therapy among elderly patients with atrial fibrillation. Circulation 2007, 115:2689-2696.
    • (2007) Circulation , vol.115 , pp. 2689-2696
    • Hylek, E.M.1    Molina, C.E.2    Shea, C.3    Henault, L.E.4    Regan, S.5
  • 137
    • 0033028757 scopus 로고    scopus 로고
    • Inhibitory effects of bovine lactoferrin on colon carcinoma 26 lung metastasis in mice
    • Iigo M., Kuhara T., Ushida Y., Sekine K., Moore M.A., Tsuda H. Inhibitory effects of bovine lactoferrin on colon carcinoma 26 lung metastasis in mice. Clin Exp Metastasis 1999, 17(1):35-40.
    • (1999) Clin Exp Metastasis , vol.17 , Issue.1 , pp. 35-40
    • Iigo, M.1    Kuhara, T.2    Ushida, Y.3    Sekine, K.4    Moore, M.A.5    Tsuda, H.6
  • 138
    • 33748758968 scopus 로고    scopus 로고
    • Cardamonin inhibits COX and iNOS expression via inhibition of p65NF-κB nuclear translocation and Iκ-B phosphorylation in RAW 264.7 macrophage cells
    • Israf D.A., Khaizurin T.A., Syahida A., Lajis N.H., Khozirah S. Cardamonin inhibits COX and iNOS expression via inhibition of p65NF-κB nuclear translocation and Iκ-B phosphorylation in RAW 264.7 macrophage cells. Mol Immunol 2007, 44:673-679.
    • (2007) Mol Immunol , vol.44 , pp. 673-679
    • Israf, D.A.1    Khaizurin, T.A.2    Syahida, A.3    Lajis, N.H.4    Khozirah, S.5
  • 139
    • 79151484740 scopus 로고    scopus 로고
    • Atrovirinone inhibits proinflammatory mediator synthesis through disruption of NF-kB nuclear translocation and MAPK phosphorylation in the murine monocytic macrophage RAW264.7
    • Israf D.A., Tham C.L., Syahida A., Lajis N.H., Sulaiman M.R., Mohamad A.S., et al. Atrovirinone inhibits proinflammatory mediator synthesis through disruption of NF-kB nuclear translocation and MAPK phosphorylation in the murine monocytic macrophage RAW264.7. Phytomedicine 2010, 17:732-739.
    • (2010) Phytomedicine , vol.17 , pp. 732-739
    • Israf, D.A.1    Tham, C.L.2    Syahida, A.3    Lajis, N.H.4    Sulaiman, M.R.5    Mohamad, A.S.6
  • 140
    • 75749122983 scopus 로고    scopus 로고
    • Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate
    • Jamdar S.N., Rajalakshmi V., Pednekar M.D., Juan F., Yardi V., Sharma A. Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate. Food Chem 2010, 121:178-184.
    • (2010) Food Chem , vol.121 , pp. 178-184
    • Jamdar, S.N.1    Rajalakshmi, V.2    Pednekar, M.D.3    Juan, F.4    Yardi, V.5    Sharma, A.6
  • 141
    • 12344308529 scopus 로고    scopus 로고
    • Purification and identification of angiotensin converting enzyme inhibitory peptides from beef hydrolysates
    • Jang A., Lee M. Purification and identification of angiotensin converting enzyme inhibitory peptides from beef hydrolysates. Meat Sci 2005, 69:653-661.
    • (2005) Meat Sci , vol.69 , pp. 653-661
    • Jang, A.1    Lee, M.2
  • 142
    • 35448968595 scopus 로고    scopus 로고
    • Antimicrobial and human cancer cell cytotoxic effect of synthetic angiotensin-converting enzyme (ACE) inhibitory peptides
    • Jang A., Jo C., Kang K.-S., Lee M. Antimicrobial and human cancer cell cytotoxic effect of synthetic angiotensin-converting enzyme (ACE) inhibitory peptides. Food Chem 2008, 107:327-336.
    • (2008) Food Chem , vol.107 , pp. 327-336
    • Jang, A.1    Jo, C.2    Kang, K.-S.3    Lee, M.4
  • 143
    • 0036094451 scopus 로고    scopus 로고
    • 1,1-Diphenyl-2-picrylhydrazyl (DPPH) radical scavenging by protein hydrolyzates from tuna cooking juice
    • Jao C.L., Ko W.C. 1,1-Diphenyl-2-picrylhydrazyl (DPPH) radical scavenging by protein hydrolyzates from tuna cooking juice. Fish Sci 2002, 68:430-435.
    • (2002) Fish Sci , vol.68 , pp. 430-435
    • Jao, C.L.1    Ko, W.C.2
  • 144
    • 11144233214 scopus 로고    scopus 로고
    • A novel angiotensin I converting enzyme inhibitory peptide from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate
    • Je J.-Y., Park P.-J., Kwon J.Y., Kim S.K. A novel angiotensin I converting enzyme inhibitory peptide from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate. J Agric Food Chem 2004, 52:7842-7845.
    • (2004) J Agric Food Chem , vol.52 , pp. 7842-7845
    • Je, J.-Y.1    Park, P.-J.2    Kwon, J.Y.3    Kim, S.K.4
  • 145
    • 22644441738 scopus 로고    scopus 로고
    • Preparation and antioxidative activity of hoki frame protein hydrolysate using ultrafiltration membranes
    • Je J.Y., Kim S.Y., Kim S.K. Preparation and antioxidative activity of hoki frame protein hydrolysate using ultrafiltration membranes. Eur Food Res Technol 2005, 221:157-162.
    • (2005) Eur Food Res Technol , vol.221 , pp. 157-162
    • Je, J.Y.1    Kim, S.Y.2    Kim, S.K.3
  • 146
    • 7444222906 scopus 로고    scopus 로고
    • Antioxidant activity of a peptide isolated from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate
    • Je J.Y., Park P.J., Kim S.K. Antioxidant activity of a peptide isolated from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate. Food Res Int 2005, 38:45-50.
    • (2005) Food Res Int , vol.38 , pp. 45-50
    • Je, J.Y.1    Park, P.J.2    Kim, S.K.3
  • 147
    • 34047153515 scopus 로고    scopus 로고
    • Purification and characterization of an antioxidant peptide obtained from tuna backbone protein by enzymatic hydrolysis
    • Je J.-Y., Qian Z.-J., Byun H.-G., Kim S.-K. Purification and characterization of an antioxidant peptide obtained from tuna backbone protein by enzymatic hydrolysis. Process Biochem 2007, 42:840-846.
    • (2007) Process Biochem , vol.42 , pp. 840-846
    • Je, J.-Y.1    Qian, Z.-J.2    Byun, H.-G.3    Kim, S.-K.4
  • 148
    • 0032727216 scopus 로고    scopus 로고
    • Improvement of functional properties of cod frame protein hydrolysates using ultrafiltration membranes
    • Jeon Y.J., Byun H.G., Kim S.K. Improvement of functional properties of cod frame protein hydrolysates using ultrafiltration membranes. Process Biochem 1999, 35:471-478.
    • (1999) Process Biochem , vol.35 , pp. 471-478
    • Jeon, Y.J.1    Byun, H.G.2    Kim, S.K.3
  • 149
    • 70349835623 scopus 로고    scopus 로고
    • The use of ultrasound for enzymatic preparation of ACE-inhibitory peptides from wheat germ protein
    • Jia J., Maa H., Zhao W., Wang Z., Tian W., Luo L., et al. The use of ultrasound for enzymatic preparation of ACE-inhibitory peptides from wheat germ protein. Food Chem 2010, 119:336-342.
    • (2010) Food Chem , vol.119 , pp. 336-342
    • Jia, J.1    Maa, H.2    Zhao, W.3    Wang, Z.4    Tian, W.5    Luo, L.6
  • 150
    • 77954620363 scopus 로고    scopus 로고
    • Production, analysis and in vivo evaluation of novel angiotensin-I-converting enzyme inhibitory peptides from bovine casein
    • Jiang Z., Tian B., Brodkorb A., Huo G. Production, analysis and in vivo evaluation of novel angiotensin-I-converting enzyme inhibitory peptides from bovine casein. Food Chem 2010, 123:779-786.
    • (2010) Food Chem , vol.123 , pp. 779-786
    • Jiang, Z.1    Tian, B.2    Brodkorb, A.3    Huo, G.4
  • 151
    • 78049435251 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from arachin by simulated gastric digestion
    • Jimsheena V.K., Gowda L.R. Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from arachin by simulated gastric digestion. Food Chem 2011, 125:561-569.
    • (2011) Food Chem , vol.125 , pp. 561-569
    • Jimsheena, V.K.1    Gowda, L.R.2
  • 153
    • 1842428894 scopus 로고    scopus 로고
    • Kinetic model for whey protein hydrolysis by alcalase multipointimmobilized on agarose gel particles
    • Jr R.S., Lopes G.P., Tardioli P.W., Giordano R.L.C., Almeida P.I.F., Giordano R.C. Kinetic model for whey protein hydrolysis by alcalase multipointimmobilized on agarose gel particles. Braz J Chem Eng 2004, 21(2):147-153.
    • (2004) Braz J Chem Eng , vol.21 , Issue.2 , pp. 147-153
    • Jr, R.S.1    Lopes, G.P.2    Tardioli, P.W.3    Giordano, R.L.C.4    Almeida, P.I.F.5    Giordano, R.C.6
  • 154
    • 7444234213 scopus 로고    scopus 로고
    • Purification and characterization of an antioxidant peptide from enzymatic hydrolysate of yellowfin sole (Limanda aspera) frame protein
    • Jun S.Y., Park P.J., Jung W.K., Kim S.K. Purification and characterization of an antioxidant peptide from enzymatic hydrolysate of yellowfin sole (Limanda aspera) frame protein. Eur Food Res Technol 2004, 219:20-26.
    • (2004) Eur Food Res Technol , vol.219 , pp. 20-26
    • Jun, S.Y.1    Park, P.J.2    Jung, W.K.3    Kim, S.K.4
  • 156
    • 67649336586 scopus 로고    scopus 로고
    • Isolation and characterization of an anticoagulant oligopeptide from blue mussel, Mytilus edulis
    • Jung W.-K., Kim S.-K. Isolation and characterization of an anticoagulant oligopeptide from blue mussel, Mytilus edulis. Food Chem 2009, 117:687-692.
    • (2009) Food Chem , vol.117 , pp. 687-692
    • Jung, W.-K.1    Kim, S.-K.2
  • 157
    • 21544467786 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptide from yellowfin sole (Limanda aspera) frame protein and its antihypertensive effect in spontaneously hypertensive rats
    • Jung W.-K., Mendis E., Je J.-Y., Park P.-J., Wha S.B., Kim H.C., et al. Angiotensin I-converting enzyme inhibitory peptide from yellowfin sole (Limanda aspera) frame protein and its antihypertensive effect in spontaneously hypertensive rats. Food Chem 2006, 94:26-32.
    • (2006) Food Chem , vol.94 , pp. 26-32
    • Jung, W.-K.1    Mendis, E.2    Je, J.-Y.3    Park, P.-J.4    Wha, S.B.5    Kim, H.C.6
  • 158
    • 34248184975 scopus 로고    scopus 로고
    • Free radical scavenging activity of a novel antioxidative peptide isolated from in vitro gastrointestinal digests of Mytilus coruscus
    • Jung W.-K., Qian Z.-J., Lee S.-H., Choi S.-Y., Sung N.-J., Byun H.-G., et al. Free radical scavenging activity of a novel antioxidative peptide isolated from in vitro gastrointestinal digests of Mytilus coruscus. J Med Food 2007, 10:197-202.
    • (2007) J Med Food , vol.10 , pp. 197-202
    • Jung, W.-K.1    Qian, Z.-J.2    Lee, S.-H.3    Choi, S.-Y.4    Sung, N.-J.5    Byun, H.-G.6
  • 159
    • 35348842113 scopus 로고    scopus 로고
    • A novel anticoagulant protein with high affinity to blood coagulation factor Va from Tegillarca granosa
    • Jung W.-K., Jo H.-Y., Qian Z.-J., Jeong Y.-J., Park S.-G., Choi I.-W., et al. A novel anticoagulant protein with high affinity to blood coagulation factor Va from Tegillarca granosa. J Biochem Mol Biol 2007, 40:832-838.
    • (2007) J Biochem Mol Biol , vol.40 , pp. 832-838
    • Jung, W.-K.1    Jo, H.-Y.2    Qian, Z.-J.3    Jeong, Y.-J.4    Park, S.-G.5    Choi, I.-W.6
  • 160
    • 77956545132 scopus 로고    scopus 로고
    • Theoretical study of the temperature dependence of dynamic effects in thymidylate synthase
    • Kanaan N., Roca M., Tunon I., Marti S., Moliner V. Theoretical study of the temperature dependence of dynamic effects in thymidylate synthase. Phys Chem Chem Phys 2010, 12:11657-11664.
    • (2010) Phys Chem Chem Phys , vol.12 , pp. 11657-11664
    • Kanaan, N.1    Roca, M.2    Tunon, I.3    Marti, S.4    Moliner, V.5
  • 161
    • 34548684339 scopus 로고    scopus 로고
    • PEPstr: a de novo method for tertiary structure prediction of small bioactive peptides
    • Kaur H., Garg A., Raghava G.P.S. PEPstr: a de novo method for tertiary structure prediction of small bioactive peptides. Protein Pept Lett 2007, 14:626-631.
    • (2007) Protein Pept Lett , vol.14 , pp. 626-631
    • Kaur, H.1    Garg, A.2    Raghava, G.P.S.3
  • 162
    • 0029924099 scopus 로고    scopus 로고
    • Stimulation of human peripheral lymphocytes by bioactive peptides derived from bovine milk proteins
    • Kayser H., Meisel H. Stimulation of human peripheral lymphocytes by bioactive peptides derived from bovine milk proteins. FEBS Lett 1996, 383:18-20.
    • (1996) FEBS Lett , vol.383 , pp. 18-20
    • Kayser, H.1    Meisel, H.2
  • 163
    • 77349090649 scopus 로고    scopus 로고
    • Development and biological activities of marine-derived bioactive peptides: a review
    • Kim S.K., Wijesekara I. Development and biological activities of marine-derived bioactive peptides: a review. J Funct Foods 2010, 2:1-9.
    • (2010) J Funct Foods , vol.2 , pp. 1-9
    • Kim, S.K.1    Wijesekara, I.2
  • 164
    • 0035595131 scopus 로고    scopus 로고
    • Purification and characterization of antioxidative peptides from bovine skin
    • Kim S.K., Kim Y.T., Byun H.G., Park P.J., Ito H. Purification and characterization of antioxidative peptides from bovine skin. J Biochem Mol Biol 2001, 34:214-219.
    • (2001) J Biochem Mol Biol , vol.34 , pp. 214-219
    • Kim, S.K.1    Kim, Y.T.2    Byun, H.G.3    Park, P.J.4    Ito, H.5
  • 165
    • 0034861073 scopus 로고    scopus 로고
    • Isolation and characterization of antioxidative peptides from gelatin hydrolysate of Alaska pollack skin
    • Kim S.K., Kim Y.T., Byun H.G., Nam K.S., Joo D.S., Shahidi F. Isolation and characterization of antioxidative peptides from gelatin hydrolysate of Alaska pollack skin. J Agric Food Chem 2001, 49:1984-1989.
    • (2001) J Agric Food Chem , vol.49 , pp. 1984-1989
    • Kim, S.K.1    Kim, Y.T.2    Byun, H.G.3    Nam, K.S.4    Joo, D.S.5    Shahidi, F.6
  • 166
    • 34548258046 scopus 로고    scopus 로고
    • Purification and characterization of antioxidant peptide from hoki (Johnius belengerii) frame protein by gastrointestinal digestion
    • Kim S.-Y., Je J.-Y., Kim S.-K. Purification and characterization of antioxidant peptide from hoki (Johnius belengerii) frame protein by gastrointestinal digestion. J Nutr Biochem 2007, 18:31-38.
    • (2007) J Nutr Biochem , vol.18 , pp. 31-38
    • Kim, S.-Y.1    Je, J.-Y.2    Kim, S.-K.3
  • 167
    • 84930483374 scopus 로고    scopus 로고
    • Purification of a novel anticancer peptide from enzymatic hydrolysate of Mytilus coruscus
    • Kim E.K., Joung H.J., Kim Y.S., Hwang J.W., Ahn C.B., Jeon Y.J., et al. Purification of a novel anticancer peptide from enzymatic hydrolysate of Mytilus coruscus. J Microbial Biotechnol 2012, 22(10):1381-1387.
    • (2012) J Microbial Biotechnol , vol.22 , Issue.10 , pp. 1381-1387
    • Kim, E.K.1    Joung, H.J.2    Kim, Y.S.3    Hwang, J.W.4    Ahn, C.B.5    Jeon, Y.J.6
  • 168
    • 0038058742 scopus 로고    scopus 로고
    • Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery
    • Kitts D.D., Weiler K. Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery. Curr Pharm Des 2003, 9(16):1309-1323.
    • (2003) Curr Pharm Des , vol.9 , Issue.16 , pp. 1309-1323
    • Kitts, D.D.1    Weiler, K.2
  • 169
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • Klibanov A.M. Improving enzymes by using them in organic solvents. Nature 2001, 409:241-246.
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 170
    • 33846610587 scopus 로고    scopus 로고
    • Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type
    • Klompong V., Benjakul S., Kantachote D., Shahidi F. Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type. Food Chem 2007, 102(4):1317-1327.
    • (2007) Food Chem , vol.102 , Issue.4 , pp. 1317-1327
    • Klompong, V.1    Benjakul, S.2    Kantachote, D.3    Shahidi, F.4
  • 171
    • 43449129718 scopus 로고    scopus 로고
    • Comparative study on antioxidative activity of yellow stripe trevally protein hydrolysate produced from Alcalase and Flavourzyme
    • Klompong V., Benjakul S., Kantachote D., Hayes K.D., Shahidi F. Comparative study on antioxidative activity of yellow stripe trevally protein hydrolysate produced from Alcalase and Flavourzyme. Int J Food Sci Tech 2008, 43(6):1019-1026.
    • (2008) Int J Food Sci Tech , vol.43 , Issue.6 , pp. 1019-1026
    • Klompong, V.1    Benjakul, S.2    Kantachote, D.3    Hayes, K.D.4    Shahidi, F.5
  • 172
    • 32444437104 scopus 로고    scopus 로고
    • Absorption-enhancing treatments for antihypertensive activity of oligopeptides from tuna cooking juice: In vivo evaluation in spontaneously hypertensive rats
    • Ko W.-C., Cheng M.-L., Hsu K.-C., Hwang J.-S. Absorption-enhancing treatments for antihypertensive activity of oligopeptides from tuna cooking juice: In vivo evaluation in spontaneously hypertensive rats. J Food Sci 2006, 71(1):13-17.
    • (2006) J Food Sci , vol.71 , Issue.1 , pp. 13-17
    • Ko, W.-C.1    Cheng, M.-L.2    Hsu, K.-C.3    Hwang, J.-S.4
  • 173
    • 33646351088 scopus 로고    scopus 로고
    • Identification of an Angiotensin I-converting enzyme inhibitory peptides from protein hydrolysates by a soybean protease and the antihypertensive effects of hydrolysates in spontaneously hypertensive model rats
    • Kodera T., Nio N. Identification of an Angiotensin I-converting enzyme inhibitory peptides from protein hydrolysates by a soybean protease and the antihypertensive effects of hydrolysates in spontaneously hypertensive model rats. J Food Sci 2006, 71(3):164-173.
    • (2006) J Food Sci , vol.71 , Issue.3 , pp. 164-173
    • Kodera, T.1    Nio, N.2
  • 174
    • 33748431810 scopus 로고    scopus 로고
    • Antioxidant activity of zein hydrolysates in a liposome system and the possible mode of action
    • Kong B., Xiong Y.L. Antioxidant activity of zein hydrolysates in a liposome system and the possible mode of action. J Agric Food Chem 2006, 54:6059-6068.
    • (2006) J Agric Food Chem , vol.54 , pp. 6059-6068
    • Kong, B.1    Xiong, Y.L.2
  • 175
    • 50349093170 scopus 로고    scopus 로고
    • Enzymatic preparation of immunomodulating hydrolysates from soy proteins
    • Kong X.Z., Guo M.M., Hua Y.F., Cao D., Zhang C.M. Enzymatic preparation of immunomodulating hydrolysates from soy proteins. Bioresour Technol 2008, 99:8873-8879.
    • (2008) Bioresour Technol , vol.99 , pp. 8873-8879
    • Kong, X.Z.1    Guo, M.M.2    Hua, Y.F.3    Cao, D.4    Zhang, C.M.5
  • 176
    • 64549156088 scopus 로고    scopus 로고
    • Milk-derived bioactive peptides: from science to applications
    • Korhonen H. Milk-derived bioactive peptides: from science to applications. J Funct Foods 2009, 1:177-187.
    • (2009) J Funct Foods , vol.1 , pp. 177-187
    • Korhonen, H.1
  • 177
    • 22944459274 scopus 로고    scopus 로고
    • Bioactive peptides: novel applications for milk proteins
    • Korhonen H., Pihlanto A. Bioactive peptides: novel applications for milk proteins. Appl Biotechnol Food Sci Policy 2003, 1:133-144.
    • (2003) Appl Biotechnol Food Sci Policy , vol.1 , pp. 133-144
    • Korhonen, H.1    Pihlanto, A.2
  • 178
    • 33747503962 scopus 로고    scopus 로고
    • Review: bioactive peptides: production and functionality
    • Korhonen H., Pihlanto A. Review: bioactive peptides: production and functionality. Int Dairy J 2006, 16:945-960.
    • (2006) Int Dairy J , vol.16 , pp. 945-960
    • Korhonen, H.1    Pihlanto, A.2
  • 180
    • 0034117422 scopus 로고    scopus 로고
    • Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle hydrolyzed with various alkaline proteases
    • Kristinsson H.G., Rasco B.A. Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle hydrolyzed with various alkaline proteases. J Agric Food Chem 2000, 48:657-666.
    • (2000) J Agric Food Chem , vol.48 , pp. 657-666
    • Kristinsson, H.G.1    Rasco, B.A.2
  • 181
    • 64349124722 scopus 로고    scopus 로고
    • Antioxidative activities of some peptides isolated from hydrolyzed potato protein extract
    • Kudo K., Onodera S., Takeda Y., Benkeblia N., Shiomi N. Antioxidative activities of some peptides isolated from hydrolyzed potato protein extract. Food Chem 2009, 1(2):170-176.
    • (2009) Food Chem , vol.1 , Issue.2 , pp. 170-176
    • Kudo, K.1    Onodera, S.2    Takeda, Y.3    Benkeblia, N.4    Shiomi, N.5
  • 182
    • 0027509577 scopus 로고
    • The circulating bioactive form of human guanylin is a high molecular weight peptide (10.3kDa)
    • Kuhn M., Raida M., Aderman K., Schulz-Knappe P., Gerzerb R., Heim J.-M., et al. The circulating bioactive form of human guanylin is a high molecular weight peptide (10.3kDa). Fed Eur Biochem Soc (FEBS) 1993, 318(2):205-209.
    • (1993) Fed Eur Biochem Soc (FEBS) , vol.318 , Issue.2 , pp. 205-209
    • Kuhn, M.1    Raida, M.2    Aderman, K.3    Schulz-Knappe, P.4    Gerzerb, R.5    Heim, J.-M.6
  • 183
    • 0032437146 scopus 로고    scopus 로고
    • Direct evidence of the generation in human stomach of an antimicrobial peptide domain (lactoferricin) from ingested lactoferrin
    • Kuwata H., Yip T.T., Tomita M., Hutchens T.W. Direct evidence of the generation in human stomach of an antimicrobial peptide domain (lactoferricin) from ingested lactoferrin. Biochim Biophys Acta 1998, 1429:129-141.
    • (1998) Biochim Biophys Acta , vol.1429 , pp. 129-141
    • Kuwata, H.1    Yip, T.T.2    Tomita, M.3    Hutchens, T.W.4
  • 184
    • 0030041615 scopus 로고    scopus 로고
    • Antibacterial and immunostimulating casein-derived substances from milk: casecidin, isracidin peptides
    • Lahov E., Regelson W. Antibacterial and immunostimulating casein-derived substances from milk: casecidin, isracidin peptides. Food Chem Toxicol 1996, 34:131-145.
    • (1996) Food Chem Toxicol , vol.34 , pp. 131-145
    • Lahov, E.1    Regelson, W.2
  • 185
    • 13244277961 scopus 로고    scopus 로고
    • Preparation of antioxidant enzymatic hydrolysates from a-lactalbumin and b-lactoglobulin. Identification of active peptides by HPLC-MS/MS
    • Ledesma H.B., Dávalos A., Bartolomé B., Amigo L. Preparation of antioxidant enzymatic hydrolysates from a-lactalbumin and b-lactoglobulin. Identification of active peptides by HPLC-MS/MS. J Agric Food Chem 2005, 53:588-593.
    • (2005) J Agric Food Chem , vol.53 , pp. 588-593
    • Ledesma, H.B.1    Dávalos, A.2    Bartolomé, B.3    Amigo, L.4
  • 186
    • 0036779424 scopus 로고    scopus 로고
    • Protein drug oral delivery: the recent progress
    • Lee H.J. Protein drug oral delivery: the recent progress. Arch Pharm Res 2002, 25(5):572-584.
    • (2002) Arch Pharm Res , vol.25 , Issue.5 , pp. 572-584
    • Lee, H.J.1
  • 187
    • 0036669618 scopus 로고    scopus 로고
    • Enzyme activation for nonaqueous media
    • Lee M.-Y., Dordick J.S. Enzyme activation for nonaqueous media. Curr Opin Biotechnol 2002, 13:376-384.
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 376-384
    • Lee, M.-Y.1    Dordick, J.S.2
  • 188
    • 33646018330 scopus 로고    scopus 로고
    • Tyr-Pro-Lys, an angiotensin I-converting enzyme inhibitory peptide derived from broccoli (Brassica oleracea Italica)
    • Lee J.-E., Bae I.Y., Lee H.G., Yang C.-B. Tyr-Pro-Lys, an angiotensin I-converting enzyme inhibitory peptide derived from broccoli (Brassica oleracea Italica). Food Chem 2006, 99:143-148.
    • (2006) Food Chem , vol.99 , pp. 143-148
    • Lee, J.-E.1    Bae, I.Y.2    Lee, H.G.3    Yang, C.-B.4
  • 189
    • 67650269402 scopus 로고    scopus 로고
    • Purification and characterization of angiotensin I converting enzyme inhibitory peptides from the rotifer, Brachionus rotundiformis
    • Lee J.K., Hong S., Jeon J.K., Kim S.K., Byun H.G. Purification and characterization of angiotensin I converting enzyme inhibitory peptides from the rotifer, Brachionus rotundiformis. Bioresour Technol 2009, 100:5255-5259.
    • (2009) Bioresour Technol , vol.100 , pp. 5255-5259
    • Lee, J.K.1    Hong, S.2    Jeon, J.K.3    Kim, S.K.4    Byun, H.G.5
  • 190
    • 68349102047 scopus 로고    scopus 로고
    • A novel angiotensin I converting enzyme inhibitory peptide from tuna frame protein hydrolysate and its antihypertensive effect in spontaneously hypertensive rats
    • Lee S.-H., Qian Z.-J., Kim S.-K. A novel angiotensin I converting enzyme inhibitory peptide from tuna frame protein hydrolysate and its antihypertensive effect in spontaneously hypertensive rats. Food Chem 2010, 118:96-102.
    • (2010) Food Chem , vol.118 , pp. 96-102
    • Lee, S.-H.1    Qian, Z.-J.2    Kim, S.-K.3
  • 191
    • 77953292323 scopus 로고    scopus 로고
    • Purification and characterisation of an antioxidative peptide from enzymatic hydrolysates of duck processing by-products
    • Lee S.-J., Kim E.-K., Hwang J.-W., Oh H.-J., Cheong S.-H., Moon S.-H., et al. Purification and characterisation of an antioxidative peptide from enzymatic hydrolysates of duck processing by-products. Food Chem 2010, 123:216-220.
    • (2010) Food Chem , vol.123 , pp. 216-220
    • Lee, S.-J.1    Kim, E.-K.2    Hwang, J.-W.3    Oh, H.-J.4    Cheong, S.-H.5    Moon, S.-H.6
  • 192
    • 33744933929 scopus 로고    scopus 로고
    • Antitumor activity of the antimicrobial peptide magainin II against bladder cancer cell lines
    • Lehmann J., Retz M., Sidhu S.S., Suttmann H., Sell M., Paulsen F., et al. Antitumor activity of the antimicrobial peptide magainin II against bladder cancer cell lines. Eur Urol 2006, 50(1):141-147.
    • (2006) Eur Urol , vol.50 , Issue.1 , pp. 141-147
    • Lehmann, J.1    Retz, M.2    Sidhu, S.S.3    Suttmann, H.4    Sell, M.5    Paulsen, F.6
  • 193
    • 0035985643 scopus 로고    scopus 로고
    • Latent production of angiotensin I-converting enzyme inhibitors from buckwheat protein
    • Li C., Matsui T., Matsumoto K., Yamasaki R., Kawasaki T. Latent production of angiotensin I-converting enzyme inhibitors from buckwheat protein. J Pept Sci 2002, 8(6):267-274.
    • (2002) J Pept Sci , vol.8 , Issue.6 , pp. 267-274
    • Li, C.1    Matsui, T.2    Matsumoto, K.3    Yamasaki, R.4    Kawasaki, T.5
  • 194
    • 3242774456 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory npeptides derived from food proteins and their physiological and pharmacological effects
    • Li G.H., Le G.W., Shi Y.H., Shrestha S. Angiotensin I-converting enzyme inhibitory npeptides derived from food proteins and their physiological and pharmacological effects. Nutr Res 2004, 24:469-486.
    • (2004) Nutr Res , vol.24 , pp. 469-486
    • Li, G.H.1    Le, G.W.2    Shi, Y.H.3    Shrestha, S.4
  • 195
    • 0037022910 scopus 로고    scopus 로고
    • Inflammation and atherosclerosis
    • Libby P., Ridker P.M., Maseri A. Inflammation and atherosclerosis. Circulation 2002, 105:1135-1143.
    • (2002) Circulation , vol.105 , pp. 1135-1143
    • Libby, P.1    Ridker, P.M.2    Maseri, A.3
  • 197
    • 77956612178 scopus 로고    scopus 로고
    • Pilot-scale production of low molecular weight peptides from corn wet milling byproducts and the antihypertensive effects in vivo and in vitro
    • Lin F., Chen L., Liang R., Zhang Z., Wang J., Cai M., et al. Pilot-scale production of low molecular weight peptides from corn wet milling byproducts and the antihypertensive effects in vivo and in vitro. Food Chem 2011, 124:801-807.
    • (2011) Food Chem , vol.124 , pp. 801-807
    • Lin, F.1    Chen, L.2    Liang, R.3    Zhang, Z.4    Wang, J.5    Cai, M.6
  • 199
    • 20844434997 scopus 로고    scopus 로고
    • Potential cell culture models for antioxidant research
    • Liu R.H., Finley J. Potential cell culture models for antioxidant research. J Agric Food Chem 2005, 53:4311-4314.
    • (2005) J Agric Food Chem , vol.53 , pp. 4311-4314
    • Liu, R.H.1    Finley, J.2
  • 200
    • 77951937691 scopus 로고    scopus 로고
    • Isolation and identification of angiotensin-converting enzyme inhibitory peptides from egg white protein hydrolysates
    • Liu J., Yu Z., Zhao W., Lin S., Wang E., Zhang Y., et al. Isolation and identification of angiotensin-converting enzyme inhibitory peptides from egg white protein hydrolysates. Food Chem 2010, 122:1159-1163.
    • (2010) Food Chem , vol.122 , pp. 1159-1163
    • Liu, J.1    Yu, Z.2    Zhao, W.3    Lin, S.4    Wang, E.5    Zhang, Y.6
  • 201
    • 75849156917 scopus 로고    scopus 로고
    • Milk proteins as vehicles for bioactives
    • Livney Y.D. Milk proteins as vehicles for bioactives. Curr Opin Colloid Interface 2010, 15:73-83.
    • (2010) Curr Opin Colloid Interface , vol.15 , pp. 73-83
    • Livney, Y.D.1
  • 202
    • 33646350312 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory activity of soy protein digests in a dynamic model system simulating the upper gastrointestinal tract
    • Lo W.M.Y., Farnworth E.R., Li-Chan E.C.Y. Angiotensin I-converting enzyme inhibitory activity of soy protein digests in a dynamic model system simulating the upper gastrointestinal tract. J Food Sci 2006, 71(3):231-237.
    • (2006) J Food Sci , vol.71 , Issue.3 , pp. 231-237
    • Lo, W.M.Y.1    Farnworth, E.R.2    Li-Chan, E.C.Y.3
  • 203
    • 33748416072 scopus 로고    scopus 로고
    • Antibacterial activity of peptides and folding variants from milk proteins
    • Lòpez-Expòsito I., Recio I. Antibacterial activity of peptides and folding variants from milk proteins. Int Dairy J 2006, 16:1294-1305.
    • (2006) Int Dairy J , vol.16 , pp. 1294-1305
    • Lòpez-Expòsito, I.1    Recio, I.2
  • 205
    • 84867734643 scopus 로고    scopus 로고
    • The soybean peptide aglycin regulates glucose homeostasis in type 2 diabetic mice via IR/IRS1 pathway
    • Lu J., Zeng Y., Hou W., Zhang S., Li L., Luo X., et al. The soybean peptide aglycin regulates glucose homeostasis in type 2 diabetic mice via IR/IRS1 pathway. J Nutr Biochem 2011, 10.1016/j.jnutbio.2011.09.007.
    • (2011) J Nutr Biochem
    • Lu, J.1    Zeng, Y.2    Hou, W.3    Zhang, S.4    Li, L.5    Luo, X.6
  • 206
    • 33750728894 scopus 로고    scopus 로고
    • Analysis of novel angiotensin-I-converting enzyme inhibitory peptides from protease-hydrolyzed marine shrimp Acetes chinensis
    • Lun H.H., Lan C.X., Yun S.C., Zhong Z.Y., Cheng Z.B. Analysis of novel angiotensin-I-converting enzyme inhibitory peptides from protease-hydrolyzed marine shrimp Acetes chinensis. J Pept Sci 2006, 12:726-733.
    • (2006) J Pept Sci , vol.12 , pp. 726-733
    • Lun, H.H.1    Lan, C.X.2    Yun, S.C.3    Zhong, Z.Y.4    Cheng, Z.B.5
  • 207
    • 27144546035 scopus 로고    scopus 로고
    • Purification and identification of angiotensin I-converting enzyme inhibitory peptide from buckwheat (Fagopyrum esculentum Moench)
    • Ma M.-S., Bae I.Y., Lee H.G., Yang C.-B. Purification and identification of angiotensin I-converting enzyme inhibitory peptide from buckwheat (Fagopyrum esculentum Moench). Food Chem 2006, 96:36-42.
    • (2006) Food Chem , vol.96 , pp. 36-42
    • Ma, M.-S.1    Bae, I.Y.2    Lee, H.G.3    Yang, C.-B.4
  • 208
    • 69349093534 scopus 로고    scopus 로고
    • Fractionation and evaluation of radical scavenging peptides from in vitro digests of buckwheat protein
    • Ma Y., Xiong Y.L., Zhai J., Zhu H., Dziubla T. Fractionation and evaluation of radical scavenging peptides from in vitro digests of buckwheat protein. Food Chem 2010, 118:582-588.
    • (2010) Food Chem , vol.118 , pp. 582-588
    • Ma, Y.1    Xiong, Y.L.2    Zhai, J.3    Zhu, H.4    Dziubla, T.5
  • 209
    • 34250883860 scopus 로고    scopus 로고
    • Bovine lactoferricin causes apoptosis in Jurkat T-leukemia cells by sequential permeabilization of the cell membrane and targeting of mitochondria
    • Mader J.S., Richardson A., Salsman J., Top D., de Antueno R., Duncan R., et al. Bovine lactoferricin causes apoptosis in Jurkat T-leukemia cells by sequential permeabilization of the cell membrane and targeting of mitochondria. Exp Cell Res 2007, 313:2634-2650.
    • (2007) Exp Cell Res , vol.313 , pp. 2634-2650
    • Mader, J.S.1    Richardson, A.2    Salsman, J.3    Top, D.4    de Antueno, R.5    Duncan, R.6
  • 210
    • 79551543469 scopus 로고    scopus 로고
    • Purification and characterisation of angiotensin I converting enzyme (ACE) inhibitory peptides derived from enzymatic hydrolysate of ovotransferrin
    • Majumder K., Wu J. Purification and characterisation of angiotensin I converting enzyme (ACE) inhibitory peptides derived from enzymatic hydrolysate of ovotransferrin. Food Chem 2011, 126:1614-1619.
    • (2011) Food Chem , vol.126 , pp. 1614-1619
    • Majumder, K.1    Wu, J.2
  • 211
  • 212
    • 33947517284 scopus 로고    scopus 로고
    • Value-added utilization of yak milk casein for the production of angiotensin-I-converting enzyme inhibitory peptides
    • Mao X.-Y., Ni J.-R., Sun W.-L., Hao P.-P., Fan L. Value-added utilization of yak milk casein for the production of angiotensin-I-converting enzyme inhibitory peptides. Food Chem 2007, 103:1282-1287.
    • (2007) Food Chem , vol.103 , pp. 1282-1287
    • Mao, X.-Y.1    Ni, J.-R.2    Sun, W.-L.3    Hao, P.-P.4    Fan, L.5
  • 213
    • 0033851093 scopus 로고    scopus 로고
    • Purification and characterization of sago starch-degrading glucoamylase from Acremonium sp. endophytic fungus
    • Marlida Y., Saari N., Hassan Z., Radu S., Bakar J. Purification and characterization of sago starch-degrading glucoamylase from Acremonium sp. endophytic fungus. Food Chem 2000, 71(2):221-227.
    • (2000) Food Chem , vol.71 , Issue.2 , pp. 221-227
    • Marlida, Y.1    Saari, N.2    Hassan, Z.3    Radu, S.4    Bakar, J.5
  • 214
    • 0034307507 scopus 로고    scopus 로고
    • Improvement in raw sago starch degrading enzyme production from Acremonium sp. endophytic fungus using carbon and nitrogen sources
    • Marlida Y., Saari N., Hassan Z., Radu S. Improvement in raw sago starch degrading enzyme production from Acremonium sp. endophytic fungus using carbon and nitrogen sources. Enzyme Microb Technol 2000, 27:511-515.
    • (2000) Enzyme Microb Technol , vol.27 , pp. 511-515
    • Marlida, Y.1    Saari, N.2    Hassan, Z.3    Radu, S.4
  • 215
    • 0344061539 scopus 로고    scopus 로고
    • Tryptic hydrolysis of k{cyrillic}-caseinomacropeptide: control of the enzymatic reaction in a continuous membrane reactor
    • Martin-Orue C., Henry G., Bouhallab S. Tryptic hydrolysis of k{cyrillic}-caseinomacropeptide: control of the enzymatic reaction in a continuous membrane reactor. Enzyme Microbiol Technol 1999, 24:173-180.
    • (1999) Enzyme Microbiol Technol , vol.24 , pp. 173-180
    • Martin-Orue, C.1    Henry, G.2    Bouhallab, S.3
  • 216
    • 33746565284 scopus 로고    scopus 로고
    • Apolipoprotein E, cholesterol metabolism, diabetes, and the convergence of risk factors for Alzheimer's disease and cardiovascular disease
    • Martins I.J., Hone E., Foster J.K., Sünram-Lea S.I., Gnjec A., Fuller S.J., et al. Apolipoprotein E, cholesterol metabolism, diabetes, and the convergence of risk factors for Alzheimer's disease and cardiovascular disease. Mol Psychiatry 2006, 11:721-736.
    • (2006) Mol Psychiatry , vol.11 , pp. 721-736
    • Martins, I.J.1    Hone, E.2    Foster, J.K.3    Sünram-Lea, S.I.4    Gnjec, A.5    Fuller, S.J.6
  • 217
    • 33748749054 scopus 로고    scopus 로고
    • How does the radical-scavenging activity of soy protein food change during heating?
    • Matoba T. How does the radical-scavenging activity of soy protein food change during heating?. Daizu Tanpakushitsu Kenkyu 2002, 5:47-50.
    • (2002) Daizu Tanpakushitsu Kenkyu , vol.5 , pp. 47-50
    • Matoba, T.1
  • 218
    • 0028712310 scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle
    • Matsufuji H., Matsui T., Seki E., Osajima K., Nakashima M., Osajima Y. Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle. Biosci Biotechnol Biochem 1994, 58:2244-2245.
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 2244-2245
    • Matsufuji, H.1    Matsui, T.2    Seki, E.3    Osajima, K.4    Nakashima, M.5    Osajima, Y.6
  • 219
    • 0036126473 scopus 로고    scopus 로고
    • Val-Tyr as a natural antihypertensive dipeptide can be absorbed into the human circulatory blood system
    • Matsui T., Tamaya K., Seki E., Osajima K., Matsumoto K., Kawasaki T. Val-Tyr as a natural antihypertensive dipeptide can be absorbed into the human circulatory blood system. Clin Exp Pharmacol Physiol 2002, 29:204-208.
    • (2002) Clin Exp Pharmacol Physiol , vol.29 , pp. 204-208
    • Matsui, T.1    Tamaya, K.2    Seki, E.3    Osajima, K.4    Matsumoto, K.5    Kawasaki, T.6
  • 220
    • 0037120187 scopus 로고    scopus 로고
    • Chemically modified "polar patch" mutants of subtilisin in peptide synthesis with remarkably broad substrate acceptance: designing combinatorial biocatalysts
    • Matsumoto K., Davis B.G., Jones J.B. Chemically modified "polar patch" mutants of subtilisin in peptide synthesis with remarkably broad substrate acceptance: designing combinatorial biocatalysts. Chem Eur J 2002, 8:4129-4137.
    • (2002) Chem Eur J , vol.8 , pp. 4129-4137
    • Matsumoto, K.1    Davis, B.G.2    Jones, J.B.3
  • 221
    • 30344443092 scopus 로고    scopus 로고
    • Isolation and characterisation of a novel antibacterial peptide from bovine aS1-casein
    • McCann K.B., Shiell B.J., Michalski W.P., Lee A., Wan J., Roginski H., et al. Isolation and characterisation of a novel antibacterial peptide from bovine aS1-casein. Int Dairy J 2006, 16:316-323.
    • (2006) Int Dairy J , vol.16 , pp. 316-323
    • McCann, K.B.1    Shiell, B.J.2    Michalski, W.P.3    Lee, A.4    Wan, J.5    Roginski, H.6
  • 222
    • 79958826524 scopus 로고    scopus 로고
    • Protein dynamics and enzyme catalysis: insights from simulations
    • McGeagh J.D., Ranaghan K.E., Mulholland A.J. Protein dynamics and enzyme catalysis: insights from simulations. Biochim Biophys Acta 2011, 1814:1077-1092.
    • (2011) Biochim Biophys Acta , vol.1814 , pp. 1077-1092
    • McGeagh, J.D.1    Ranaghan, K.E.2    Mulholland, A.J.3
  • 223
    • 12144288141 scopus 로고    scopus 로고
    • Purification of an ACE inhibitory peptide after hydrolysis of sunflower (Helianthus annuus L.) protein isolates
    • Megías C., Yust M.D.M., Pedroche J., Lquari H., Calle N.J.G., Alaiz M., et al. Purification of an ACE inhibitory peptide after hydrolysis of sunflower (Helianthus annuus L.) protein isolates. J Agric Food Chem 2004, 52:1928-1932.
    • (2004) J Agric Food Chem , vol.52 , pp. 1928-1932
    • Megías, C.1    Yust, M.D.M.2    Pedroche, J.3    Lquari, H.4    Calle, N.J.G.5    Alaiz, M.6
  • 224
    • 0030749136 scopus 로고    scopus 로고
    • Biochemical properties of regulatory peptides derived from milk proteins
    • Meisel H. Biochemical properties of regulatory peptides derived from milk proteins. Biopolymers 1997, 43:119-128.
    • (1997) Biopolymers , vol.43 , pp. 119-128
    • Meisel, H.1
  • 225
    • 0039246617 scopus 로고    scopus 로고
    • Bioactive peptides from milk proteins: a perspective for consumers and producers
    • Meisel H. Bioactive peptides from milk proteins: a perspective for consumers and producers. Aust J Dairy Technol 2001, 56:83-91.
    • (2001) Aust J Dairy Technol , vol.56 , pp. 83-91
    • Meisel, H.1
  • 226
    • 0002350154 scopus 로고    scopus 로고
    • Casokinins as inhibitors of angiotensin-converting enzyme
    • Thieme, G. Sawatzki, B. Renner (Eds.)
    • Meisel H. Casokinins as inhibitors of angiotensin-converting enzyme. New perspectives in infant nutrition 2003, 153. Thieme. G. Sawatzki, B. Renner (Eds.).
    • (2003) New perspectives in infant nutrition , pp. 153
    • Meisel, H.1
  • 227
    • 0038397187 scopus 로고    scopus 로고
    • Biofunctional peptides from milk proteins: mineral binding and cytomodulatory effects
    • Meisel H., FitzGerald R.J. Biofunctional peptides from milk proteins: mineral binding and cytomodulatory effects. Curr Pharm Des 2003, 9:1289-1295.
    • (2003) Curr Pharm Des , vol.9 , pp. 1289-1295
    • Meisel, H.1    FitzGerald, R.J.2
  • 228
    • 84922939455 scopus 로고    scopus 로고
    • Investigation of jumbo squid (Dosidicus gigas) skin gelatin peptides for their in vitro antioxidant effects
    • Mendis E., Rajapakse N., Byun H.G., Kim S.K. Investigation of jumbo squid (Dosidicus gigas) skin gelatin peptides for their in vitro antioxidant effects. Life Sci 2005, 70:651-656.
    • (2005) Life Sci , vol.70 , pp. 651-656
    • Mendis, E.1    Rajapakse, N.2    Byun, H.G.3    Kim, S.K.4
  • 229
    • 13244279441 scopus 로고    scopus 로고
    • Antioxidant properties of a radicals scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate
    • Mendis E., Rajapakse N., Kim S.K. Antioxidant properties of a radicals scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate. J Agric Food Chem 2005, 53:581-587.
    • (2005) J Agric Food Chem , vol.53 , pp. 581-587
    • Mendis, E.1    Rajapakse, N.2    Kim, S.K.3
  • 230
    • 0000870544 scopus 로고
    • Die kinetik der invertinwirkung
    • Michaelis L., Menton M. Die kinetik der invertinwirkung. Biochem Z 1913, 49:333-369.
    • (1913) Biochem Z , vol.49 , pp. 333-369
    • Michaelis, L.1    Menton, M.2
  • 231
    • 38049048162 scopus 로고    scopus 로고
    • Vascular effects, angiotensin I-converting enzyme (ACE)-inhibitory activity, and antihypertensive properties of peptides derived from egg white
    • Miguel M., Manso M., Aleixandre A., Alonso M.J., Salaices M., Lopez-Fandino R. Vascular effects, angiotensin I-converting enzyme (ACE)-inhibitory activity, and antihypertensive properties of peptides derived from egg white. J Agric Food Chem 2007, 55:10615.
    • (2007) J Agric Food Chem , vol.55 , pp. 10615
    • Miguel, M.1    Manso, M.2    Aleixandre, A.3    Alonso, M.J.4    Salaices, M.5    Lopez-Fandino, R.6
  • 232
    • 57549088511 scopus 로고    scopus 로고
    • Transepithelial transport across Caco-2 cell monolayers of antihypertensive egg-derived peptides, PepT1-mediated flux of Tyr-Pro-Ile
    • Miguel M., Dávalos A., Manso M.A., de la Peña G., Lasuncion M.A., Lopez-Fandino R. Transepithelial transport across Caco-2 cell monolayers of antihypertensive egg-derived peptides, PepT1-mediated flux of Tyr-Pro-Ile. Mol Nutr Food Res 2008, 52:1507-1513.
    • (2008) Mol Nutr Food Res , vol.52 , pp. 1507-1513
    • Miguel, M.1    Dávalos, A.2    Manso, M.A.3    de la Peña, G.4    Lasuncion, M.A.5    Lopez-Fandino, R.6
  • 233
    • 0036768546 scopus 로고    scopus 로고
    • Activation of remaining key enzymes in dried under-fermented cocoa beans and its effect on aroma precursor formation
    • Misnawi, Selamat J., Saari N., Bakar J. Activation of remaining key enzymes in dried under-fermented cocoa beans and its effect on aroma precursor formation. Food Chem 2002, 78(4):407-417.
    • (2002) Food Chem , vol.78 , Issue.4 , pp. 407-417
    • Misnawi, S.J.1    Saari, N.2    Bakar, J.3
  • 234
    • 0037248710 scopus 로고    scopus 로고
    • Establishment of T cell lines to bovine β-casein and β-casein-derived epitopes in patients with type 1 diabetes
    • Monetini L., Barone F., Stefanini L., Petrone A., Walk T., Jung G., et al. Establishment of T cell lines to bovine β-casein and β-casein-derived epitopes in patients with type 1 diabetes. J Endocrinol 2003, 176:143-150.
    • (2003) J Endocrinol , vol.176 , pp. 143-150
    • Monetini, L.1    Barone, F.2    Stefanini, L.3    Petrone, A.4    Walk, T.5    Jung, G.6
  • 235
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 1983, 65:55-63.
    • (1983) J Immunol Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 236
    • 0242467926 scopus 로고    scopus 로고
    • Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides from wheat gliadin hydrolysate
    • Motoi H., Kodama T. Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides from wheat gliadin hydrolysate. Nahrung/Food 2003, 47(5):354-358.
    • (2003) Nahrung/Food , vol.47 , Issue.5 , pp. 354-358
    • Motoi, H.1    Kodama, T.2
  • 237
    • 26244468929 scopus 로고    scopus 로고
    • Fractionation and enzymatic hydrolysis of soluble protein present in waste liquors from soy processing
    • Moure A., Domínguez H., Parajó J.C. Fractionation and enzymatic hydrolysis of soluble protein present in waste liquors from soy processing. J Agric Food Chem 2005, 53:7600-7608.
    • (2005) J Agric Food Chem , vol.53 , pp. 7600-7608
    • Moure, A.1    Domínguez, H.2    Parajó, J.C.3
  • 238
    • 0009662259 scopus 로고
    • Hormone isolation
    • Churchill Ltvingstone, Edinburgh, London, New York, S.R. Bloom (Ed.)
    • Mutt V. Hormone isolation. Gut hormones 1978, 21-27. Churchill Ltvingstone, Edinburgh, London, New York. S.R. Bloom (Ed.).
    • (1978) Gut hormones , pp. 21-27
    • Mutt, V.1
  • 239
    • 74849087802 scopus 로고    scopus 로고
    • Antihypertensive effect of peptide-enriched soy sauce-like seasoning and identification of its angiotensin I-converting enzyme inhibitory substances
    • Nakahara T., Sano A., Yamaguchi H., Sugimoto K.R.I., Chikata H., Kinoshita E., et al. Antihypertensive effect of peptide-enriched soy sauce-like seasoning and identification of its angiotensin I-converting enzyme inhibitory substances. J Agric Food Chem 2010, 58:821.
    • (2010) J Agric Food Chem , vol.58 , pp. 821
    • Nakahara, T.1    Sano, A.2    Yamaguchi, H.3    Sugimoto, K.R.I.4    Chikata, H.5    Kinoshita, E.6
  • 240
    • 33646816054 scopus 로고    scopus 로고
    • Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides from a sesame protein hydrolysate in spontaneously hypertensive rats
    • Nakano D., Ogura K., Miyakoshi M., Ishii F., Kawanishi H., Kurumazuka D., et al. Antihypertensive effect of angiotensin I-converting enzyme inhibitory peptides from a sesame protein hydrolysate in spontaneously hypertensive rats. Biosci Biotechnol Biochem 2006, 70:1118.
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 1118
    • Nakano, D.1    Ogura, K.2    Miyakoshi, M.3    Ishii, F.4    Kawanishi, H.5    Kurumazuka, D.6
  • 242
    • 84882767015 scopus 로고    scopus 로고
    • ACE inhibitory and antioxidative activities of Goby (Zosterissessor ophiocephalus) fish protein hydrolysates: effect on meat lipid oxidation
    • Nasri R., Younes I., Jridi M., Trigui M., Bougatef A., Nedjar-Arroume N., et al. ACE inhibitory and antioxidative activities of Goby (Zosterissessor ophiocephalus) fish protein hydrolysates: effect on meat lipid oxidation. Food Res Int 2013, 54:552-561.
    • (2013) Food Res Int , vol.54 , pp. 552-561
    • Nasri, R.1    Younes, I.2    Jridi, M.3    Trigui, M.4    Bougatef, A.5    Nedjar-Arroume, N.6
  • 243
    • 84883535390 scopus 로고    scopus 로고
    • Novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of goby (Zosterisessor ophiocephalus) muscle proteins
    • Nasri R., Chataigné G., Bougatef A., Chaâbouni M.K., Dhulster P., Nasri M., et al. Novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of goby (Zosterisessor ophiocephalus) muscle proteins. J Proteomics 2013, 91:444-452.
    • (2013) J Proteomics , vol.91 , pp. 444-452
    • Nasri, R.1    Chataigné, G.2    Bougatef, A.3    Chaâbouni, M.K.4    Dhulster, P.5    Nasri, M.6
  • 244
    • 0346195665 scopus 로고    scopus 로고
    • Crystal structure of the human angiotensin-converting enzyme-lisinopril complex
    • Natesh R., Schwager S.L.U., Sturrock E.D., Acharya K.R. Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature 2003, 421:551.
    • (2003) Nature , vol.421 , pp. 551
    • Natesh, R.1    Schwager, S.L.U.2    Sturrock, E.D.3    Acharya, K.R.4
  • 245
    • 79952314733 scopus 로고    scopus 로고
    • Marine food-derived functional ingredients as potential antioxidants in the food industry: an overview
    • Ngo D.H., Wijesekara I., Vo T.S., Ta Q.V., Kim S.-K. Marine food-derived functional ingredients as potential antioxidants in the food industry: an overview. Food Res Int 2011, 44(2):523-529.
    • (2011) Food Res Int , vol.44 , Issue.2 , pp. 523-529
    • Ngo, D.H.1    Wijesekara, I.2    Vo, T.S.3    Ta, Q.V.4    Kim, S.-K.5
  • 246
    • 84859386987 scopus 로고    scopus 로고
    • Intracellular tumor-associated antigens represent effective targets for passive immunotherapy
    • Noguchi T., Kato T., Wang L., Maeda Y., Ikeda H., Sato E., et al. Intracellular tumor-associated antigens represent effective targets for passive immunotherapy. Cancer Res 2012, 72(7):1672-1682.
    • (2012) Cancer Res , vol.72 , Issue.7 , pp. 1672-1682
    • Noguchi, T.1    Kato, T.2    Wang, L.3    Maeda, Y.4    Ikeda, H.5    Sato, E.6
  • 247
    • 1642489328 scopus 로고    scopus 로고
    • Enzyme stabilization - recent experimental progress
    • Ó'Fágáin C. Enzyme stabilization - recent experimental progress. Enzyme Microb Technol 2003, 33:137-149.
    • (2003) Enzyme Microb Technol , vol.33 , pp. 137-149
    • Ó'Fágáin, C.1
  • 248
    • 3242889844 scopus 로고    scopus 로고
    • C-terminal domain of human CAP18 antimicrobial peptide induces apoptosis in oral squamous cell carcinoma SAS-H1 cells
    • Okumura K., Itoh A., Isogai E., Hirose K., Hosokawa Y., Abiko Y., et al. C-terminal domain of human CAP18 antimicrobial peptide induces apoptosis in oral squamous cell carcinoma SAS-H1 cells. Cancer Lett 2004, 212(2):185-194.
    • (2004) Cancer Lett , vol.212 , Issue.2 , pp. 185-194
    • Okumura, K.1    Itoh, A.2    Isogai, E.3    Hirose, K.4    Hosokawa, Y.5    Abiko, Y.6
  • 249
    • 33748365234 scopus 로고    scopus 로고
    • Transition state theory can be used in studies of enzyme catalysis: lessons from simulations of tunnelling and dynamical effects in lipoxygenase and other systems
    • Olsson M.H.M., Mavri J., Warshel A. Transition state theory can be used in studies of enzyme catalysis: lessons from simulations of tunnelling and dynamical effects in lipoxygenase and other systems. Philos Trans R Soc 2006, B 361:1417-1432.
    • (2006) Philos Trans R Soc , vol.B 361 , pp. 1417-1432
    • Olsson, M.H.M.1    Mavri, J.2    Warshel, A.3
  • 250
    • 33646935697 scopus 로고    scopus 로고
    • Dynamical contributions to enzyme catalysis: critical tests of a popular hypothesis
    • Olsson M.H.M., Parson W.W., Warshel A. Dynamical contributions to enzyme catalysis: critical tests of a popular hypothesis. Chem Rev 2006, 1737-1756.
    • (2006) Chem Rev , pp. 1737-1756
    • Olsson, M.H.M.1    Parson, W.W.2    Warshel, A.3
  • 251
    • 80052964449 scopus 로고    scopus 로고
    • Purification, characterization and thermal inactivation kinetics of a non-regioselective thermostable lipase from a genotypically identified extremophilic Bacillus subtilis NS 8
    • Olusesan A.T., Azura L.K., Forghani B., Abu-Bakar F., Abdul-Karim S.M., Radu S., et al. Purification, characterization and thermal inactivation kinetics of a non-regioselective thermostable lipase from a genotypically identified extremophilic Bacillus subtilis NS 8. New Biotechnol 2011, 28(6):738-745.
    • (2011) New Biotechnol , vol.28 , Issue.6 , pp. 738-745
    • Olusesan, A.T.1    Azura, L.K.2    Forghani, B.3    Abu-Bakar, F.4    Abdul-Karim, S.M.5    Radu, S.6
  • 252
    • 0021152476 scopus 로고
    • Angiotensin-converting enzyme inhibitors: biochemical properties and biological actions
    • Ondetti M.A., Cushman D.W. Angiotensin-converting enzyme inhibitors: biochemical properties and biological actions. CRC Crit Rev Biochem 1984, 16(4):381-411.
    • (1984) CRC Crit Rev Biochem , vol.16 , Issue.4 , pp. 381-411
    • Ondetti, M.A.1    Cushman, D.W.2
  • 253
    • 0017578611 scopus 로고
    • Design of specific inhibitors of angiotensin converting enzyme: new class of orally active antihypertensive agents
    • Ondetti M.A., Rubin B., Cushman D.W. Design of specific inhibitors of angiotensin converting enzyme: new class of orally active antihypertensive agents. Science 1977, 196:441.
    • (1977) Science , vol.196 , pp. 441
    • Ondetti, M.A.1    Rubin, B.2    Cushman, D.W.3
  • 254
    • 33644905566 scopus 로고    scopus 로고
    • Inhibition properties of dipeptides from salmon muscle hydrolysate on angiotensin I-converting enzyme
    • Ono S., Hosokawa M., Miyashita K., Takahashi K. Inhibition properties of dipeptides from salmon muscle hydrolysate on angiotensin I-converting enzyme. Int J Food Sci Technol 2005, 41(4):383-386.
    • (2005) Int J Food Sci Technol , vol.41 , Issue.4 , pp. 383-386
    • Ono, S.1    Hosokawa, M.2    Miyashita, K.3    Takahashi, K.4
  • 255
    • 0346058017 scopus 로고    scopus 로고
    • Purification and characterization of membrane-bound peroxidases from Metroxylon sagu
    • Onsa G.H., Saari N., Selamat J., Bakar J. Purification and characterization of membrane-bound peroxidases from Metroxylon sagu. Food Chem 2004, 85(3):365-376.
    • (2004) Food Chem , vol.85 , Issue.3 , pp. 365-376
    • Onsa, G.H.1    Saari, N.2    Selamat, J.3    Bakar, J.4
  • 256
    • 68849100746 scopus 로고    scopus 로고
    • Evaluation of cross linked aggregates from purified Bacillus subtilis levansucrase mutants for transfructosylation reactions
    • Ortiz-Soto M.E., Rudiño-Piñera E., Rodriguez-Alegria M.E., Munguia A.L. Evaluation of cross linked aggregates from purified Bacillus subtilis levansucrase mutants for transfructosylation reactions. BMC Biotech 2009, 9(68):1-8.
    • (2009) BMC Biotech , vol.9 , Issue.68 , pp. 1-8
    • Ortiz-Soto, M.E.1    Rudiño-Piñera, E.2    Rodriguez-Alegria, M.E.3    Munguia, A.L.4
  • 257
    • 0029294541 scopus 로고
    • Inhibition of proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells by bovine milk caseins and their digests
    • Otani H., Hata I. Inhibition of proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells by bovine milk caseins and their digests. J Dairy Res 1995, 62(2):339-348.
    • (1995) J Dairy Res , vol.62 , Issue.2 , pp. 339-348
    • Otani, H.1    Hata, I.2
  • 259
    • 9644277040 scopus 로고    scopus 로고
    • Antihypertensive peptides from skimmed milk hydrolysate digested by cell-free extract of Lactobacillus helveticus JCM1004
    • Pan D., Luo Y., Tanokura M. Antihypertensive peptides from skimmed milk hydrolysate digested by cell-free extract of Lactobacillus helveticus JCM1004. Food Chem 2005, 91:123-129.
    • (2005) Food Chem , vol.91 , pp. 123-129
    • Pan, D.1    Luo, Y.2    Tanokura, M.3
  • 260
    • 80051782220 scopus 로고    scopus 로고
    • Studies on purification and the molecular mechanism of a novel ACE inhibitory peptide from whey protein hydrolysate
    • Pan D., Cao J., Guo H., Zhao B. Studies on purification and the molecular mechanism of a novel ACE inhibitory peptide from whey protein hydrolysate. Food Chem 2011, 100(1):121-126.
    • (2011) Food Chem , vol.100 , Issue.1 , pp. 121-126
    • Pan, D.1    Cao, J.2    Guo, H.3    Zhao, B.4
  • 261
    • 80051782220 scopus 로고    scopus 로고
    • Studies on purification and the molecular mechanism of a novel ACE inhibitory peptide from whey protein hydrolysate
    • Pan D., Cao J., Guo H., Zhao B. Studies on purification and the molecular mechanism of a novel ACE inhibitory peptide from whey protein hydrolysate. Food Chem 2012, 130:121-126.
    • (2012) Food Chem , vol.130 , pp. 121-126
    • Pan, D.1    Cao, J.2    Guo, H.3    Zhao, B.4
  • 262
    • 0026758933 scopus 로고
    • Transmucosal impedance of small intestine - correlation with transport of sugars and amino acids
    • Pappenheimer J.R., Volpp K. Transmucosal impedance of small intestine - correlation with transport of sugars and amino acids. Am J Physiol 1992, 263:C480-C493.
    • (1992) Am J Physiol , vol.263 , pp. C480-C493
    • Pappenheimer, J.R.1    Volpp, K.2
  • 263
    • 0035358387 scopus 로고    scopus 로고
    • Purification and characterization of antioxidative peptides from lecithin-free egg yolk protein
    • Park P.J., Jung W.K., Nam K.S., Shahidi F., Kim S.K. Purification and characterization of antioxidative peptides from lecithin-free egg yolk protein. J Am Oil Chem Soc 2001, 78:651-656.
    • (2001) J Am Oil Chem Soc , vol.78 , pp. 651-656
    • Park, P.J.1    Jung, W.K.2    Nam, K.S.3    Shahidi, F.4    Kim, S.K.5
  • 264
    • 2442700307 scopus 로고    scopus 로고
    • Antioxidant activities of enzymatic extracts from an edible seaweed sargassum horneri using ESR spectrometry
    • Park P.-J., Shahidi F., Jeon Y.-J. Antioxidant activities of enzymatic extracts from an edible seaweed sargassum horneri using ESR spectrometry. J Food Lipids 2004, 11(1):15-27.
    • (2004) J Food Lipids , vol.11 , Issue.1 , pp. 15-27
    • Park, P.-J.1    Shahidi, F.2    Jeon, Y.-J.3
  • 265
    • 0021677121 scopus 로고
    • Immunostimulating hexapeptide from human casein: amino acid sequence, synthesis and biological properties
    • Parker F., Migliore-Samour D., Floc'h F., Zerail A., Werner G.H., Jollès J., et al. Immunostimulating hexapeptide from human casein: amino acid sequence, synthesis and biological properties. Eur J Biochem 1984, 45:677-682.
    • (1984) Eur J Biochem , vol.45 , pp. 677-682
    • Parker, F.1    Migliore-Samour, D.2    Floc'h, F.3    Zerail, A.4    Werner, G.H.5    Jollès, J.6
  • 266
    • 0023782745 scopus 로고
    • Opioid peptides from food (the Exorphins)
    • Paroli E. Opioid peptides from food (the Exorphins). World Rev Nutr Diet 1988, 55:58-97.
    • (1988) World Rev Nutr Diet , vol.55 , pp. 58-97
    • Paroli, E.1
  • 267
    • 79959213588 scopus 로고    scopus 로고
    • Colloidal delivery systems in foods: a general comparison with oral drug delivery
    • Patel A.R., Velikov K.P. Colloidal delivery systems in foods: a general comparison with oral drug delivery. LWT-Food Sci Technol 2011, 44:1958-1964.
    • (2011) LWT-Food Sci Technol , vol.44 , pp. 1958-1964
    • Patel, A.R.1    Velikov, K.P.2
  • 268
    • 52949091925 scopus 로고    scopus 로고
    • Antioxidant activity of peptide fractions from whey protein hydrolysates as measured by electron spin resonance
    • Peng X., Xiong Y.L., Kong B. Antioxidant activity of peptide fractions from whey protein hydrolysates as measured by electron spin resonance. Food Chem 2009, 113(1):196-201.
    • (2009) Food Chem , vol.113 , Issue.1 , pp. 196-201
    • Peng, X.1    Xiong, Y.L.2    Kong, B.3
  • 269
    • 0036813306 scopus 로고    scopus 로고
    • Antioxidant activity of soy protein hydrolyzates in a liposomial system
    • Peña-Ramos E.A., Xiong Y.L. Antioxidant activity of soy protein hydrolyzates in a liposomial system. J Food Sci 2002, 67:2952-2956.
    • (2002) J Food Sci , vol.67 , pp. 2952-2956
    • Peña-Ramos, E.A.1    Xiong, Y.L.2
  • 270
    • 0035425380 scopus 로고    scopus 로고
    • Enzyme catalysis: removing chemically 'essential' residues by site-directed mutagenesis
    • Peracchi A. Enzyme catalysis: removing chemically 'essential' residues by site-directed mutagenesis. Trends Biochem Sci 2001, 26(8):497-503.
    • (2001) Trends Biochem Sci , vol.26 , Issue.8 , pp. 497-503
    • Peracchi, A.1
  • 271
    • 18244416412 scopus 로고    scopus 로고
    • ID(ϕ, ψ), to analyze the contribution of rotating moieties to the shape of potential energy surfaces
    • ID(ϕ, ψ), to analyze the contribution of rotating moieties to the shape of potential energy surfaces. J Mol Struct (Theochem) 2000, 500:59-96.
    • (2000) J Mol Struct (Theochem) , vol.500 , pp. 59-96
    • Perczel, A.1    Hudaky, P.2    Csizmadia, I.G.3
  • 272
    • 0030024410 scopus 로고    scopus 로고
    • Continuous hydrolysis of whey proteins in a membrane recycle reactor
    • Perea A., Ugalde U. Continuous hydrolysis of whey proteins in a membrane recycle reactor. Enzyme Microbiol Technol 1996, 18:29-34.
    • (1996) Enzyme Microbiol Technol , vol.18 , pp. 29-34
    • Perea, A.1    Ugalde, U.2
  • 273
    • 0020321280 scopus 로고
    • Angiotensin-converting enzyme inhibitors: medicinal chemistry and biological action
    • Petrillo E.W., Ondetti M.A. Angiotensin-converting enzyme inhibitors: medicinal chemistry and biological action. Med Res Rev 1982, 2(1):1-41.
    • (1982) Med Res Rev , vol.2 , Issue.1 , pp. 1-41
    • Petrillo, E.W.1    Ondetti, M.A.2
  • 274
    • 69349102184 scopus 로고    scopus 로고
    • Casein-derived bioactive peptides: Biological effects, industrial uses, safety aspects and regulatory status
    • Phelan M., Aherne A., FitzGerald R.J., O'Brien N.M. Casein-derived bioactive peptides: Biological effects, industrial uses, safety aspects and regulatory status. Int Dairy J 2009, 19(11):643-654.
    • (2009) Int Dairy J , vol.19 , Issue.11 , pp. 643-654
    • Phelan, M.1    Aherne, A.2    FitzGerald, R.J.3    O'Brien, N.M.4
  • 275
    • 78649768736 scopus 로고    scopus 로고
    • Therapeutic peptides under the spotlight
    • Pichereau C., Allary C. Therapeutic peptides under the spotlight. Eur Biopharm Rev 2005, 5:1-4.
    • (2005) Eur Biopharm Rev , vol.5 , pp. 1-4
    • Pichereau, C.1    Allary, C.2
  • 276
    • 84455171399 scopus 로고    scopus 로고
    • Comparison of peptide cancer signatures identified by mass spectrometry in serum of patients with head and neck, lung and colorectal cancers: association with tumor progression
    • Pietrowska M., Polańska J., Suwiński R., Widel M., Rutkowski T., Marczyk M., et al. Comparison of peptide cancer signatures identified by mass spectrometry in serum of patients with head and neck, lung and colorectal cancers: association with tumor progression. Int J Oncol 2012, 40:148-156.
    • (2012) Int J Oncol , vol.40 , pp. 148-156
    • Pietrowska, M.1    Polańska, J.2    Suwiński, R.3    Widel, M.4    Rutkowski, T.5    Marczyk, M.6
  • 277
    • 0034633086 scopus 로고    scopus 로고
    • Bioactive peptides derived from bovine whey proteins: opioid and ace-inhibitory peptides
    • Pihlanto-Leppälä A. Bioactive peptides derived from bovine whey proteins: opioid and ace-inhibitory peptides. Trends Food Sci Technol 2001, 11:347-356.
    • (2001) Trends Food Sci Technol , vol.11 , pp. 347-356
    • Pihlanto-Leppälä, A.1
  • 278
    • 38049086022 scopus 로고    scopus 로고
    • Milk proteins j bioactive peptides
    • Elsevier, Oxford, R. Hubert (Ed.)
    • Pihlanto-Leppälä A. Milk proteins j bioactive peptides. Encyclopedia of dairy sciences 2002, 1960. Elsevier, Oxford. R. Hubert (Ed.).
    • (2002) Encyclopedia of dairy sciences , pp. 1960
    • Pihlanto-Leppälä, A.1
  • 279
    • 33846197938 scopus 로고    scopus 로고
    • Biocatalysis for pharmaceutical intermediates: the future is now
    • Pollard D.J., Woodley J.M. Biocatalysis for pharmaceutical intermediates: the future is now. Trends Biotechnol 2007, 25:66-73.
    • (2007) Trends Biotechnol , vol.25 , pp. 66-73
    • Pollard, D.J.1    Woodley, J.M.2
  • 280
    • 33846199139 scopus 로고    scopus 로고
    • Modelling relationship between angiotensin-(I)-converting enzyme inhibition and the bitter taste of peptides
    • Pripp A.H., Ardo Y. Modelling relationship between angiotensin-(I)-converting enzyme inhibition and the bitter taste of peptides. Food Chem 2007, 102:880-888.
    • (2007) Food Chem , vol.102 , pp. 880-888
    • Pripp, A.H.1    Ardo, Y.2
  • 281
    • 35548970730 scopus 로고    scopus 로고
    • Antihypertensive effect of angiotensin I converting enzyme-inhibitory peptide from hydrolysates of bigeye tuna dark muscle, thunnus obesus
    • Qian Z.J., Je J.-Y., Kim S.-K. Antihypertensive effect of angiotensin I converting enzyme-inhibitory peptide from hydrolysates of bigeye tuna dark muscle, thunnus obesus. J Agric Food Chem 2007, 55:8398-8403.
    • (2007) J Agric Food Chem , vol.55 , pp. 8398-8403
    • Qian, Z.J.1    Je, J.-Y.2    Kim, S.-K.3
  • 282
    • 37549036223 scopus 로고    scopus 로고
    • Free radical scavenging activity of a novel antioxidative peptide purified from hydrolysate of bullfrog skin, Rana catesbeiana Shaw
    • Qian Z.J., Jung W.K., Kim S.K. Free radical scavenging activity of a novel antioxidative peptide purified from hydrolysate of bullfrog skin, Rana catesbeiana Shaw. Bioresour Technol 2008, 99:1690-1698.
    • (2008) Bioresour Technol , vol.99 , pp. 1690-1698
    • Qian, Z.J.1    Jung, W.K.2    Kim, S.K.3
  • 283
    • 79952804303 scopus 로고    scopus 로고
    • Antioxidant, antihypertensive, and immunomodulatory activities of peptide fractions from fermented skim milk with Lactobacillus delbrueckii ssp. bulgaricus LB340
    • Qian B., Xing M., Cui L., Deng Y., Xu Y., Huang M., et al. Antioxidant, antihypertensive, and immunomodulatory activities of peptide fractions from fermented skim milk with Lactobacillus delbrueckii ssp. bulgaricus LB340. J Dairy Res 2011, 78:72-79.
    • (2011) J Dairy Res , vol.78 , pp. 72-79
    • Qian, B.1    Xing, M.2    Cui, L.3    Deng, Y.4    Xu, Y.5    Huang, M.6
  • 284
    • 77952585562 scopus 로고    scopus 로고
    • Preparation and antihypertensive activity of peptides from Porphyra yezoensis
    • Qu W., Ma H., Pan Z., Luo L., Wang Z., He R. Preparation and antihypertensive activity of peptides from Porphyra yezoensis. Food Chem 2010, 123:14-20.
    • (2010) Food Chem , vol.123 , pp. 14-20
    • Qu, W.1    Ma, H.2    Pan, Z.3    Luo, L.4    Wang, Z.5    He, R.6
  • 285
    • 68049101085 scopus 로고    scopus 로고
    • Application of label-free quantitative peptidomics for the identification of urinary biomarkers of kidney chronic allograft dysfunction
    • Quintana L.F., Campistol J.M., Alcolea M.P., Banon-Maneus E., Sol-Gonzalez A., Cutillas P.R. Application of label-free quantitative peptidomics for the identification of urinary biomarkers of kidney chronic allograft dysfunction. Mol Cell Proteomics 2009, 8:1658-1673.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1658-1673
    • Quintana, L.F.1    Campistol, J.M.2    Alcolea, M.P.3    Banon-Maneus, E.4    Sol-Gonzalez, A.5    Cutillas, P.R.6
  • 286
    • 0028918401 scopus 로고
    • A proficient enzyme
    • Radzicka A., Wolfenden R. A proficient enzyme. Science 1995, 267:90-93.
    • (1995) Science , vol.267 , pp. 90-93
    • Radzicka, A.1    Wolfenden, R.2
  • 287
    • 23944469378 scopus 로고    scopus 로고
    • Purification and in vitro antioxidative effects of giant squid muscle peptides on free radical-mediated oxidative systems
    • Rajapakse N., Mendis E., Byun H.G., Kim S.K. Purification and in vitro antioxidative effects of giant squid muscle peptides on free radical-mediated oxidative systems. J Nutr Biochem 2005, 16:562-569.
    • (2005) J Nutr Biochem , vol.16 , pp. 562-569
    • Rajapakse, N.1    Mendis, E.2    Byun, H.G.3    Kim, S.K.4
  • 288
    • 11144293558 scopus 로고    scopus 로고
    • Purification of a radical scavenging peptide from fermented mussel sauce and its antioxidant properties
    • Rajapakse N., Mendis E., Jung W.K., Je J.Y., Kim S.K. Purification of a radical scavenging peptide from fermented mussel sauce and its antioxidant properties. Food Res Int 2005, 38:175-182.
    • (2005) Food Res Int , vol.38 , pp. 175-182
    • Rajapakse, N.1    Mendis, E.2    Jung, W.K.3    Je, J.Y.4    Kim, S.K.5
  • 289
    • 14844359987 scopus 로고    scopus 로고
    • Anticoagulant derived from fish protein hydrolysate inhibits factor Xlla and platelet aggregation
    • Rajapakse N., Jung W.K., Mendis E., Moon S.H., Kim S.K. Anticoagulant derived from fish protein hydrolysate inhibits factor Xlla and platelet aggregation. Life Sci 2005, 76:2607-2619.
    • (2005) Life Sci , vol.76 , pp. 2607-2619
    • Rajapakse, N.1    Jung, W.K.2    Mendis, E.3    Moon, S.H.4    Kim, S.K.5
  • 290
    • 79955575033 scopus 로고    scopus 로고
    • Yogurt can beneficially affect blood contributors of cardiovascular health status in hypertensive rats
    • Ramchandran L., Shah N.P. Yogurt can beneficially affect blood contributors of cardiovascular health status in hypertensive rats. J Food Sci 2011, 76(4):131-136.
    • (2011) J Food Sci , vol.76 , Issue.4 , pp. 131-136
    • Ramchandran, L.1    Shah, N.P.2
  • 291
    • 32244443027 scopus 로고    scopus 로고
    • Purification and characterization of antioxidative peptide derived from muscle of conger eel (Conger myriaster)
    • Ranathunga S., Rajapakse N., Kim S.K. Purification and characterization of antioxidative peptide derived from muscle of conger eel (Conger myriaster). Eur Food Res Technol 2006, 222:310-315.
    • (2006) Eur Food Res Technol , vol.222 , pp. 310-315
    • Ranathunga, S.1    Rajapakse, N.2    Kim, S.K.3
  • 293
    • 38049034404 scopus 로고    scopus 로고
    • Purification and identification of antioxidant peptides from grass carp hydrolysates by consecutive chromatography and electrospray ionization-mass spectrometry
    • Ren J., Zhao M., Shi J., Wang J., Jiang Y., Cui C., et al. Purification and identification of antioxidant peptides from grass carp hydrolysates by consecutive chromatography and electrospray ionization-mass spectrometry. Food Chem 2008, 108:727-736.
    • (2008) Food Chem , vol.108 , pp. 727-736
    • Ren, J.1    Zhao, M.2    Shi, J.3    Wang, J.4    Jiang, Y.5    Cui, C.6
  • 294
    • 0035136024 scopus 로고    scopus 로고
    • Caseins and casein hydrolysates. II. Antioxidative properties and relevance to lipoxygenase inhibition
    • Rival S.G., Boeriu C.G., Wichers H.J. Caseins and casein hydrolysates. II. Antioxidative properties and relevance to lipoxygenase inhibition. J Agric Food Chem 2001, 49:295-302.
    • (2001) J Agric Food Chem , vol.49 , pp. 295-302
    • Rival, S.G.1    Boeriu, C.G.2    Wichers, H.J.3
  • 295
    • 0035134979 scopus 로고    scopus 로고
    • Caseins and casein hydrolysates. I. Lipoxygenase inhibitory properties
    • Rival S.G., Fornaroli S., Boeriu C.G., Wichers H.J. Caseins and casein hydrolysates. I. Lipoxygenase inhibitory properties. J Agric Food Chem 2001, 49:287-294.
    • (2001) J Agric Food Chem , vol.49 , pp. 287-294
    • Rival, S.G.1    Fornaroli, S.2    Boeriu, C.G.3    Wichers, H.J.4
  • 296
    • 34249318078 scopus 로고    scopus 로고
    • Effects of pulsed electric fields on water-soluble vitamins and ACE inhibitory peptides added to a mixed orange juice and milk beverage
    • Rivas A., Rodrigo D., Company B., Sampedro F., Rodrigo M. Effects of pulsed electric fields on water-soluble vitamins and ACE inhibitory peptides added to a mixed orange juice and milk beverage. Food Chem 2007, 104:1550-1559.
    • (2007) Food Chem , vol.104 , pp. 1550-1559
    • Rivas, A.1    Rodrigo, D.2    Company, B.3    Sampedro, F.4    Rodrigo, M.5
  • 297
    • 0033007311 scopus 로고    scopus 로고
    • Effect of chain length on absorption of biologically active peptides from the gastrointestinal tract
    • Roberts P.R., Burney J.D., Black K.W., Zaloga G.P. Effect of chain length on absorption of biologically active peptides from the gastrointestinal tract. Digestion 1999, 60:332-337.
    • (1999) Digestion , vol.60 , pp. 332-337
    • Roberts, P.R.1    Burney, J.D.2    Black, K.W.3    Zaloga, G.P.4
  • 298
    • 33644825853 scopus 로고    scopus 로고
    • Testing the nature of the Lambda (1520)-resonance in proton-induced production
    • Roca L., Hanhart C., Oset E., Meissner U.G. Testing the nature of the Lambda (1520)-resonance in proton-induced production. Eur Phys J A 2006, 27:373-380.
    • (2006) Eur Phys J A , vol.27 , pp. 373-380
    • Roca, L.1    Hanhart, C.2    Oset, E.3    Meissner, U.G.4
  • 300
    • 0040511030 scopus 로고    scopus 로고
    • Release of bioactive peptides by enzymatic proteolysis of Lactobacillus GG fermented UHT-milk
    • Rokka T., Syväoja E.-L., Tuominen J., Korhonen H. Release of bioactive peptides by enzymatic proteolysis of Lactobacillus GG fermented UHT-milk. Milchwissenschaft 1997, 52:675-678.
    • (1997) Milchwissenschaft , vol.52 , pp. 675-678
    • Rokka, T.1    Syväoja, E.-L.2    Tuominen, J.3    Korhonen, H.4
  • 301
    • 77958139106 scopus 로고    scopus 로고
    • Kinetics of hydrolysis of egg white protein by pepsin
    • Ruan Ch.-Q., Chi Y.-J., Zhang R.-D. Kinetics of hydrolysis of egg white protein by pepsin. Czech J Food Sci 2010, 28:355-363.
    • (2010) Czech J Food Sci , vol.28 , pp. 355-363
    • Ruan, C.-Q.1    Chi, Y.-J.2    Zhang, R.-D.3
  • 302
    • 0026190477 scopus 로고
    • Gastrointestinal lymphatic absorption of peptides and proteins
    • Rubas W., Grass G.M. Gastrointestinal lymphatic absorption of peptides and proteins. Adv Drug Deliv Rev 1991, 7:15-69.
    • (1991) Adv Drug Deliv Rev , vol.7 , pp. 15-69
    • Rubas, W.1    Grass, G.M.2
  • 303
    • 44949134134 scopus 로고    scopus 로고
    • Dynamic effects on reaction rates in a Michael addition catalyzed by chalcone isomerase: beyond the frozen environment approach
    • Ruiz-Pernia J.J., Tunon I., Moliner V., Hynes J.T., Roca M. Dynamic effects on reaction rates in a Michael addition catalyzed by chalcone isomerase: beyond the frozen environment approach. J Am Chem Soc 2008, 130:7477-7488.
    • (2008) J Am Chem Soc , vol.130 , pp. 7477-7488
    • Ruiz-Pernia, J.J.1    Tunon, I.2    Moliner, V.3    Hynes, J.T.4    Roca, M.5
  • 304
    • 34347346201 scopus 로고    scopus 로고
    • Protein immobilization strategies for protein biochips
    • Rusmini F., Zhong Z., Feijen J. Protein immobilization strategies for protein biochips. Biomacromolecules 2007, 8:1775-1789.
    • (2007) Biomacromolecules , vol.8 , pp. 1775-1789
    • Rusmini, F.1    Zhong, Z.2    Feijen, J.3
  • 306
    • 0344958843 scopus 로고    scopus 로고
    • Ascorbate oxidase from starfruit (Averrhoa carambola): preparation and its application in the determination of ascorbic acid from fruit juices
    • Saari N., Osman A., Selamat J., Fujita S. Ascorbate oxidase from starfruit (Averrhoa carambola): preparation and its application in the determination of ascorbic acid from fruit juices. Food Chem 1999, 66:57-61.
    • (1999) Food Chem , vol.66 , pp. 57-61
    • Saari, N.1    Osman, A.2    Selamat, J.3    Fujita, S.4
  • 307
    • 43649089507 scopus 로고    scopus 로고
    • Les microesferas comosistemas de liberación controlada de péptidos y proteínas (Microspheres as delevery systems for the controlled release of peptides and protiens)
    • Saenz V., Ramón J., Peniche C. Les microesferas comosistemas de liberación controlada de péptidos y proteínas (Microspheres as delevery systems for the controlled release of peptides and protiens). Biotecnol Apl 2007, 24:98-107.
    • (2007) Biotecnol Apl , vol.24 , pp. 98-107
    • Saenz, V.1    Ramón, J.2    Peniche, C.3
  • 308
    • 0344951108 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides in a hydrolyzed chicken breast muscle extract
    • Saiga A., Okumura T., Makihara T., Katsuta S., Shimizu T., Yamada R., et al. Angiotensin I-converting enzyme inhibitory peptides in a hydrolyzed chicken breast muscle extract. J Agric Food Chem 2003, 51:1741-1745.
    • (2003) J Agric Food Chem , vol.51 , pp. 1741-1745
    • Saiga, A.1    Okumura, T.2    Makihara, T.3    Katsuta, S.4    Shimizu, T.5    Yamada, R.6
  • 309
    • 33244454977 scopus 로고    scopus 로고
    • Action mechanism of an angiotensin I-converting enzyme inhibitory peptide derived from chicken breast muscle
    • Saiga A., Okumura T., Makihara T., Katsuda S.I., Morimatsu F., Nishimura T. Action mechanism of an angiotensin I-converting enzyme inhibitory peptide derived from chicken breast muscle. J Agric Food Chem 2006, 54:942-945.
    • (2006) J Agric Food Chem , vol.54 , pp. 942-945
    • Saiga, A.1    Okumura, T.2    Makihara, T.3    Katsuda, S.I.4    Morimatsu, F.5    Nishimura, T.6
  • 310
    • 0038689280 scopus 로고    scopus 로고
    • Antioxidative properties of tripeptide libraries prepared by the combinatorial chemistry
    • Saito K., Jin D.H., Ogawa T., Muramoto K., Hatakeyama E., Yasuhara T., et al. Antioxidative properties of tripeptide libraries prepared by the combinatorial chemistry. J Agric Food Chem 2003, 51:3668-3674.
    • (2003) J Agric Food Chem , vol.51 , pp. 3668-3674
    • Saito, K.1    Jin, D.H.2    Ogawa, T.3    Muramoto, K.4    Hatakeyama, E.5    Yasuhara, T.6
  • 311
    • 36448964429 scopus 로고    scopus 로고
    • Immunomodulating properties of a whey protein isolate, its enzymatic digest and peptide fractions
    • Saint-Sauveur D., Gauthier S.F., Boutin Y., Montoni A. Immunomodulating properties of a whey protein isolate, its enzymatic digest and peptide fractions. Int Dairy J 2008, 18:260-270.
    • (2008) Int Dairy J , vol.18 , pp. 260-270
    • Saint-Sauveur, D.1    Gauthier, S.F.2    Boutin, Y.3    Montoni, A.4
  • 312
    • 77956688199 scopus 로고    scopus 로고
    • Antioxidative peptides from food proteins: A review
    • Sarmadi B.H., Ismail A. Antioxidative peptides from food proteins: A review. Peptides 2010, 31:1949-1956.
    • (2010) Peptides , vol.31 , pp. 1949-1956
    • Sarmadi, B.H.1    Ismail, A.2
  • 313
    • 84866363079 scopus 로고    scopus 로고
    • Bio-functionalities of proteins derived from marine algae - a review
    • Samarakoon K., Jeon Y.-J. Bio-functionalities of proteins derived from marine algae - a review. Food Res Int 2012, 48:948-960.
    • (2012) Food Res Int , vol.48 , pp. 948-960
    • Samarakoon, K.1    Jeon, Y.-J.2
  • 314
    • 80052259929 scopus 로고    scopus 로고
    • Food-derived peptidic antioxidants: a review of their production, assessment, and potential applications
    • Samaranayaka A.G.P., Li-Chan E.C.Y. Food-derived peptidic antioxidants: a review of their production, assessment, and potential applications. J Funct Foods 2011, 4(3):229-254.
    • (2011) J Funct Foods , vol.4 , Issue.3 , pp. 229-254
    • Samaranayaka, A.G.P.1    Li-Chan, E.C.Y.2
  • 315
    • 0035169059 scopus 로고    scopus 로고
    • A peptide derived from bovine β-casein modulates functional properties of bone marrow-derived macrophages from germfree and human floraassociated mice
    • Sandre C., Gleizes A., Forestier F., Gorges-Kergot R., Chilmonczyk S., Léonil J., et al. A peptide derived from bovine β-casein modulates functional properties of bone marrow-derived macrophages from germfree and human floraassociated mice. J Nutr 2001, 131:2936-2942.
    • (2001) J Nutr , vol.131 , pp. 2936-2942
    • Sandre, C.1    Gleizes, A.2    Forestier, F.3    Gorges-Kergot, R.4    Chilmonczyk, S.5    Léonil, J.6
  • 317
    • 84922866728 scopus 로고    scopus 로고
    • Transepithelial transport of the bioactive tripeptide, Val-Pro-Pro, in human intestinal Caco-2 cell lines
    • Satake M., Enjoh M., Nakamura Y., Takano T., Kawamura Y., Arai S., et al. Transepithelial transport of the bioactive tripeptide, Val-Pro-Pro, in human intestinal Caco-2 cell lines. Biochem Pharmacol 2002, 70:1796-1806.
    • (2002) Biochem Pharmacol , vol.70 , pp. 1796-1806
    • Satake, M.1    Enjoh, M.2    Nakamura, Y.3    Takano, T.4    Kawamura, Y.5    Arai, S.6
  • 318
    • 0037048736 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides derived from Wakame (Undaria pinnatifida) and their antihypertensive effect in spontaneously hypertensive rats
    • Sato M., Hosokawa T., Yamaguchi T., Nakano T., Muramoto K., Kahara T., et al. Angiotensin I-converting enzyme inhibitory peptides derived from Wakame (Undaria pinnatifida) and their antihypertensive effect in spontaneously hypertensive rats. J Agric Food Chem 2002, 50:6245-6252.
    • (2002) J Agric Food Chem , vol.50 , pp. 6245-6252
    • Sato, M.1    Hosokawa, T.2    Yamaguchi, T.3    Nakano, T.4    Muramoto, K.5    Kahara, T.6
  • 322
    • 84859090757 scopus 로고    scopus 로고
    • Bioactive peptides: a review
    • Sharma S., Singh R., Rana S. Bioactive peptides: a review. Int J Bioautom 2011, 15(4):223-250.
    • (2011) Int J Bioautom , vol.15 , Issue.4 , pp. 223-250
    • Sharma, S.1    Singh, R.2    Rana, S.3
  • 323
    • 47249145097 scopus 로고    scopus 로고
    • Efficient immobilization of Lecitase in Gelatin hydrogel and degumming of rice bran oil using a spinning basket reactor
    • Sheelu G., Kavitha G., Fadnavis N.W. Efficient immobilization of Lecitase in Gelatin hydrogel and degumming of rice bran oil using a spinning basket reactor. J Am Oil Chem Soc 2008, 85:739-748.
    • (2008) J Am Oil Chem Soc , vol.85 , pp. 739-748
    • Sheelu, G.1    Kavitha, G.2    Fadnavis, N.W.3
  • 324
    • 63449096537 scopus 로고    scopus 로고
    • Antioxidant properties of a new antioxidative peptide from algae protein waste hydrolysate in different oxidation systems
    • Sheih I.C., Wu T.K., Fang T.J. Antioxidant properties of a new antioxidative peptide from algae protein waste hydrolysate in different oxidation systems. Bioresour Technol 2009, 100:3419-3425.
    • (2009) Bioresour Technol , vol.100 , pp. 3419-3425
    • Sheih, I.C.1    Wu, T.K.2    Fang, T.J.3
  • 325
    • 19744366251 scopus 로고    scopus 로고
    • Green solvents for sustainable organic synthesis: state of the art
    • Sheldon R.A. Green solvents for sustainable organic synthesis: state of the art. Green Chem 2005, 7:267-278.
    • (2005) Green Chem , vol.7 , pp. 267-278
    • Sheldon, R.A.1
  • 327
    • 84862776705 scopus 로고    scopus 로고
    • Chitosan-based luminescent/magnetic hybrid nanogels for insulin delivery, cell imaging, and antidiabetic research of dietary supplements
    • Shen J.-M., Xu L., Lu Y., Cao H.-M., Xu Z.-G., Chen T., et al. Chitosan-based luminescent/magnetic hybrid nanogels for insulin delivery, cell imaging, and antidiabetic research of dietary supplements. Int J Pharm 2012, 10.1016/j.ijpharm.2012.01.059.
    • (2012) Int J Pharm
    • Shen, J.-M.1    Xu, L.2    Lu, Y.3    Cao, H.-M.4    Xu, Z.-G.5    Chen, T.6
  • 328
    • 2942604856 scopus 로고    scopus 로고
    • Isolation and characterization of an immunomodulatory protein (APP) from the Jew's Ear mushroom Auricularia polytricha
    • Sheu F., Chien P.-J., Chien A.-L., Chen Y.-F., Chin K.-L. Isolation and characterization of an immunomodulatory protein (APP) from the Jew's Ear mushroom Auricularia polytricha. Food Chem 2004, 87:593-600.
    • (2004) Food Chem , vol.87 , pp. 593-600
    • Sheu, F.1    Chien, P.-J.2    Chien, A.-L.3    Chen, Y.-F.4    Chin, K.-L.5
  • 329
    • 0039984257 scopus 로고    scopus 로고
    • Modulation of intestinal functions by food substances
    • Shimizu M. Modulation of intestinal functions by food substances. Nahrung 1999, 43:154-158.
    • (1999) Nahrung , vol.43 , pp. 154-158
    • Shimizu, M.1
  • 330
    • 0030759649 scopus 로고    scopus 로고
    • Transepithelial transport of oligopeptides in the human intestinal cell, Caco-2
    • Shimizu M., Tsunogai M., Arai S. Transepithelial transport of oligopeptides in the human intestinal cell, Caco-2. Peptides 1997, 18:681-687.
    • (1997) Peptides , vol.18 , pp. 681-687
    • Shimizu, M.1    Tsunogai, M.2    Arai, S.3
  • 335
    • 67650712906 scopus 로고
    • University of California Press, Berkeley, H. Smith (Ed.)
    • The molecular biology of plant cells 1977, University of California Press, Berkeley, (http://ark.cdlib.org/ark:/13030/ft796nb4n2/). H. Smith (Ed.).
    • (1977) The molecular biology of plant cells
  • 336
    • 0036900263 scopus 로고    scopus 로고
    • The production of fine chemicals by biotransformations
    • Straathof A.J.J., Panke S., Schmid A. The production of fine chemicals by biotransformations. Curr Opin Biotechnol 2002, 13:548-556.
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 548-556
    • Straathof, A.J.J.1    Panke, S.2    Schmid, A.3
  • 337
    • 0032124780 scopus 로고    scopus 로고
    • Isolation and characterization of angiotensin I converting enzyme inhibitor dipeptides derived from Allium sativum L. (garlic)
    • Suetsuna K. Isolation and characterization of angiotensin I converting enzyme inhibitor dipeptides derived from Allium sativum L. (garlic). J Nutr Biochem 1998, 9:415-419.
    • (1998) J Nutr Biochem , vol.9 , pp. 415-419
    • Suetsuna, K.1
  • 338
    • 22644451856 scopus 로고    scopus 로고
    • Separation and identification of antioxidant peptides from proteolytic digest of dried bonito
    • Suetsuna K. Separation and identification of antioxidant peptides from proteolytic digest of dried bonito. Nippon Suisan Gakkaishi 1999, 65:92-96.
    • (1999) Nippon Suisan Gakkaishi , vol.65 , pp. 92-96
    • Suetsuna, K.1
  • 339
    • 0033695674 scopus 로고    scopus 로고
    • Identification of an antihypertensive peptide from peptic digests of wakame (Undaria pinnatifida)
    • Suetsuna K., Nakano T. Identification of an antihypertensive peptide from peptic digests of wakame (Undaria pinnatifida). J Nutr Biochem 2000, 11:450-454.
    • (2000) J Nutr Biochem , vol.11 , pp. 450-454
    • Suetsuna, K.1    Nakano, T.2
  • 340
    • 0033268174 scopus 로고    scopus 로고
    • Isolation of an octapeptide which possesses active oxygen scavenging activity from peptic digests of sardine muscle
    • Suetsuna K., Ukeda H. Isolation of an octapeptide which possesses active oxygen scavenging activity from peptic digests of sardine muscle. Nippon Suisan Gakkaishi 1999, 65:1096-1099.
    • (1999) Nippon Suisan Gakkaishi , vol.65 , pp. 1096-1099
    • Suetsuna, K.1    Ukeda, H.2
  • 341
    • 0034101865 scopus 로고    scopus 로고
    • Isolation and characterization of free radical scavenging activities peptides derived from casein
    • Suetsuna K., Ukeda H., Ochi H. Isolation and characterization of free radical scavenging activities peptides derived from casein. J Nutr Biochem 2000, 11:128-131.
    • (2000) J Nutr Biochem , vol.11 , pp. 128-131
    • Suetsuna, K.1    Ukeda, H.2    Ochi, H.3
  • 342
    • 0037021625 scopus 로고    scopus 로고
    • Antioxidant and antiproliferative activities of common fruits
    • Sun J., Chu Y.F., Wu X.Z., Liu R.H. Antioxidant and antiproliferative activities of common fruits. J Agric Food Chem 2002, 50:7449-7454.
    • (2002) J Agric Food Chem , vol.50 , pp. 7449-7454
    • Sun, J.1    Chu, Y.F.2    Wu, X.Z.3    Liu, R.H.4
  • 343
    • 6344253204 scopus 로고    scopus 로고
    • Novel antioxidant peptides from fermented mushroom Ganoderma lucidum
    • Sun J., He H., Xie B.J. Novel antioxidant peptides from fermented mushroom Ganoderma lucidum. J Agric Food Chem 2004, 52:6646-6652.
    • (2004) J Agric Food Chem , vol.52 , pp. 6646-6652
    • Sun, J.1    He, H.2    Xie, B.J.3
  • 344
    • 0028122920 scopus 로고
    • Isolation and characterization of oryzatensin - a novel bioactive peptide with ileum-contracting and immunomodulating activities derived from rice albumin
    • Takahashi M., Moriguchi S., Yoshikawa M., Sasaki R. Isolation and characterization of oryzatensin - a novel bioactive peptide with ileum-contracting and immunomodulating activities derived from rice albumin. Biochem Mol Biol Int 1994, 33:1151-1158.
    • (1994) Biochem Mol Biol Int , vol.33 , pp. 1151-1158
    • Takahashi, M.1    Moriguchi, S.2    Yoshikawa, M.3    Sasaki, R.4
  • 345
    • 62249172972 scopus 로고    scopus 로고
    • Antihypertensive activities of royal jelly protein hydrolysate and its fractions in spontaneously hypertensive rats
    • Takai-Doi S., Hashimoto K., Yamamura M., Kamei C. Antihypertensive activities of royal jelly protein hydrolysate and its fractions in spontaneously hypertensive rats. Acta Med Okayama 2009, 63:57.
    • (2009) Acta Med Okayama , vol.63 , pp. 57
    • Takai-Doi, S.1    Hashimoto, K.2    Yamamura, M.3    Kamei, C.4
  • 346
    • 75249095753 scopus 로고    scopus 로고
    • Peptide fractionation and free radical scavenging activity of zein
    • Tang X., He Z., Dait Y., Xiong Y.L., Xie M., Chen J. Peptide fractionation and free radical scavenging activity of zein. J Agric Food Chem 2010, 58:587-593.
    • (2010) J Agric Food Chem , vol.58 , pp. 587-593
    • Tang, X.1    He, Z.2    Dait, Y.3    Xiong, Y.L.4    Xie, M.5    Chen, J.6
  • 347
    • 0030794980 scopus 로고    scopus 로고
    • Milk protein-derived opioid receptor ligands
    • Teschemacher H., Koch G., Brantl V. Milk protein-derived opioid receptor ligands. Pept Sci 1997, 43:99-117.
    • (1997) Pept Sci , vol.43 , pp. 99-117
    • Teschemacher, H.1    Koch, G.2    Brantl, V.3
  • 348
    • 0038396397 scopus 로고    scopus 로고
    • Opioid Receptor Ligands Derived from Food Proteins
    • Teschemacher H. Opioid Receptor Ligands Derived from Food Proteins. Curr Pharm Des 2003, 9:1331-1344.
    • (2003) Curr Pharm Des , vol.9 , pp. 1331-1344
    • Teschemacher, H.1
  • 349
    • 33847753820 scopus 로고    scopus 로고
    • Antioxidative activities of protein hydrolysate from round scad muscle using alcalase and flavourzyme
    • Thiansilakul Y., Benjakul S., Shahidi F. Antioxidative activities of protein hydrolysate from round scad muscle using alcalase and flavourzyme. J Food Biochem 2007, 31:266-287.
    • (2007) J Food Biochem , vol.31 , pp. 266-287
    • Thiansilakul, Y.1    Benjakul, S.2    Shahidi, F.3
  • 350
    • 65849145033 scopus 로고    scopus 로고
    • Characterization and ACE-inhibitory activity of amaranth proteins
    • Tiengo A., Faria M., Netto F.M. Characterization and ACE-inhibitory activity of amaranth proteins. J Food Sci 2009, 74(5):121-126.
    • (2009) J Food Sci , vol.74 , Issue.5 , pp. 121-126
    • Tiengo, A.1    Faria, M.2    Netto, F.M.3
  • 351
    • 0026293901 scopus 로고
    • Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin
    • Tomita M., Bellamy W., Takase M., Yamauchi K., Wakabayashi H., Kawase K. Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin. J Dairy Sci 1991, 74:4137-4142.
    • (1991) J Dairy Sci , vol.74 , pp. 4137-4142
    • Tomita, M.1    Bellamy, W.2    Takase, M.3    Yamauchi, K.4    Wakabayashi, H.5    Kawase, K.6
  • 352
    • 79959948783 scopus 로고    scopus 로고
    • Affinity purification and characterization of chelating peptides from chickpea protein hydrolysates
    • Torres-Fuentes C., Alaiz M., Vioque J. Affinity purification and characterization of chelating peptides from chickpea protein hydrolysates. Food Chem 2011, 129:485-490.
    • (2011) Food Chem , vol.129 , pp. 485-490
    • Torres-Fuentes, C.1    Alaiz, M.2    Vioque, J.3
  • 353
    • 0029636230 scopus 로고
    • Effects of sorbitol addition on the action of free and immobilized hydrolytic enzymes in organic media
    • Triantafyllou A.O., Wehtje E., Adlercreutz P., Mattiasson B. Effects of sorbitol addition on the action of free and immobilized hydrolytic enzymes in organic media. Biotechnol Bioeng 1995, 45:406-414.
    • (1995) Biotechnol Bioeng , vol.45 , pp. 406-414
    • Triantafyllou, A.O.1    Wehtje, E.2    Adlercreutz, P.3    Mattiasson, B.4
  • 354
    • 44249117319 scopus 로고    scopus 로고
    • ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria)
    • Tsai J.S., Chen J.L., Pan B.S. ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria). Process Biochem 2008, 43:743-747.
    • (2008) Process Biochem , vol.43 , pp. 743-747
    • Tsai, J.S.1    Chen, J.L.2    Pan, B.S.3
  • 357
    • 0001967529 scopus 로고
    • Sequence-dependent reactivity of histidine-containing peptides with copper (II)/ascorbate
    • Uchida K., Kawakishi S. Sequence-dependent reactivity of histidine-containing peptides with copper (II)/ascorbate. J Food Biochem 1992, 40:13-16.
    • (1992) J Food Biochem , vol.40 , pp. 13-16
    • Uchida, K.1    Kawakishi, S.2
  • 358
    • 76649139801 scopus 로고    scopus 로고
    • Mutant lipase-catalyzed kinetic resolution of bulky phenyl alkyl sec-alcohols: a thermodynamic analysis of enantioselectivity
    • Vallin M., Syrén P.-O., Hult K. Mutant lipase-catalyzed kinetic resolution of bulky phenyl alkyl sec-alcohols: a thermodynamic analysis of enantioselectivity. ChemBioChem 2010, 11(3):411-416.
    • (2010) ChemBioChem , vol.11 , Issue.3 , pp. 411-416
    • Vallin, M.1    Syrén, P.-O.2    Hult, K.3
  • 359
    • 33748887871 scopus 로고    scopus 로고
    • Caco-2 cell permeability assays to measure drug absorption
    • van Breemen R.B., Li Y. Caco-2 cell permeability assays to measure drug absorption. Expert Opin Drug Metab 2005, 1:175-185.
    • (2005) Expert Opin Drug Metab , vol.1 , pp. 175-185
    • van Breemen, R.B.1    Li, Y.2
  • 360
    • 58149477514 scopus 로고    scopus 로고
    • Improved enontioselective conversion of styrene epoxides and meso-epoxides through epoxide hydrolyses with a mutated nucleophile-flanking residue
    • Van Loo B., Kingma J., Heyman G., Wittenaar A., Spelberg J.H.L., Sonke T., Janssen D.B. Improved enontioselective conversion of styrene epoxides and meso-epoxides through epoxide hydrolyses with a mutated nucleophile-flanking residue. Enzyme Microb Technol 2009, 44:145-153.
    • (2009) Enzyme Microb Technol , vol.44 , pp. 145-153
    • Van Loo, B.1    Kingma, J.2    Heyman, G.3    Wittenaar, A.4    Spelberg, J.H.L.5    Sonke, T.6    Janssen, D.B.7
  • 361
    • 32544439415 scopus 로고    scopus 로고
    • Chemical composition of polymers surface imaged by atomic force microscopy and complementary approaches
    • Springer-Verlag, Berlin, Heidelberg, New York, S. Anantawaraskul (Ed.)
    • Vansco G.J., Hillborg H., Schönherr H. Chemical composition of polymers surface imaged by atomic force microscopy and complementary approaches. Polymer analysis and polymer theory 2005, 55-130. Springer-Verlag, Berlin, Heidelberg, New York. S. Anantawaraskul (Ed.).
    • (2005) Polymer analysis and polymer theory , pp. 55-130
    • Vansco, G.J.1    Hillborg, H.2    Schönherr, H.3
  • 362
    • 0034492053 scopus 로고    scopus 로고
    • Mineral-binding milk proteins and peptides; occurrence, biochemical and technological characteristics
    • Vegarud G.E., Langsrud T., Svenning C. Mineral-binding milk proteins and peptides; occurrence, biochemical and technological characteristics. Br J Nutr 2000, 84(Suppl. 1):S91-S98.
    • (2000) Br J Nutr , vol.84 , pp. S91-S98
    • Vegarud, G.E.1    Langsrud, T.2    Svenning, C.3
  • 364
    • 6944221879 scopus 로고    scopus 로고
    • Bioavailability of angiotensin I converting enzyme inhibitory peptides
    • Vermeirssen V., Camp J.V., Verstraete W. Bioavailability of angiotensin I converting enzyme inhibitory peptides. Br J Nutr 2004, 92:357-366.
    • (2004) Br J Nutr , vol.92 , pp. 357-366
    • Vermeirssen, V.1    Camp, J.V.2    Verstraete, W.3
  • 365
    • 31344453213 scopus 로고    scopus 로고
    • In vitro intestinal transport and antihypertensive activity of ACE inhibitory pea and whey digests
    • Vermeirssen V., Augustijns P., Van Camp J., Opsomer A., Verstraete W. In vitro intestinal transport and antihypertensive activity of ACE inhibitory pea and whey digests. Int J Food Sci Nutr 2005, 56:415-430.
    • (2005) Int J Food Sci Nutr , vol.56 , pp. 415-430
    • Vermeirssen, V.1    Augustijns, P.2    Van Camp, J.3    Opsomer, A.4    Verstraete, W.5
  • 366
    • 0036185339 scopus 로고    scopus 로고
    • Towards a structure-function analysis of bovine lactoferricin and related tryptophan and arginine containing peptides
    • Vogel H.J., Schibli D.J., Weiguo J., Lohmeier-Vogel E.M., Epand R.F., Epand R.M. Towards a structure-function analysis of bovine lactoferricin and related tryptophan and arginine containing peptides. Biochem Cell Biol 2002, 80:49-63.
    • (2002) Biochem Cell Biol , vol.80 , pp. 49-63
    • Vogel, H.J.1    Schibli, D.J.2    Weiguo, J.3    Lohmeier-Vogel, E.M.4    Epand, R.F.5    Epand, R.M.6
  • 367
    • 0030555659 scopus 로고    scopus 로고
    • Kinetics of the initial stage of milk protein hydrolysis by chymotrypsin
    • Vorob'ev M.M., Levicheva I.Y., Belikov V.M. Kinetics of the initial stage of milk protein hydrolysis by chymotrypsin. Appl Biochem Microbiol 1996, 32:219-222.
    • (1996) Appl Biochem Microbiol , vol.32 , pp. 219-222
    • Vorob'ev, M.M.1    Levicheva, I.Y.2    Belikov, V.M.3
  • 369
    • 0031035028 scopus 로고    scopus 로고
    • Differences in the pharmacokinetics of 13-CIS retinoic acid in cancer patients
    • Waladkhani A.R., Clemens M.R. Differences in the pharmacokinetics of 13-CIS retinoic acid in cancer patients. Int J Cancer 1998, 70:494-495.
    • (1998) Int J Cancer , vol.70 , pp. 494-495
    • Waladkhani, A.R.1    Clemens, M.R.2
  • 370
    • 33748747614 scopus 로고    scopus 로고
    • A new frontier in soy bioactive peptides that may prevent age-related chronic diseases
    • Wang W., de Mejia E.G. A new frontier in soy bioactive peptides that may prevent age-related chronic diseases. Compr Rev Food Sci Food Saf 2005, 4(4):63-78.
    • (2005) Compr Rev Food Sci Food Saf , vol.4 , Issue.4 , pp. 63-78
    • Wang, W.1    de Mejia, E.G.2
  • 371
    • 51749125991 scopus 로고    scopus 로고
    • Purification and identification of an ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats
    • Wang J., Hu J., Cui J., Bai X., Du Y., Miyaguchi Y., et al. Purification and identification of an ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats. Food Chem 2008, 111:302-308.
    • (2008) Food Chem , vol.111 , pp. 302-308
    • Wang, J.1    Hu, J.2    Cui, J.3    Bai, X.4    Du, Y.5    Miyaguchi, Y.6
  • 374
    • 79951647068 scopus 로고    scopus 로고
    • Biohydrogenation from biomass sugar mediated by in vitro synthetic enzymatic pathways
    • Wang Y., Huang W., Sathitsuksanoh N., Zhu Z., Zhang Y.-H.P. Biohydrogenation from biomass sugar mediated by in vitro synthetic enzymatic pathways. Chem Biol 2011, 18:372-380.
    • (2011) Chem Biol , vol.18 , pp. 372-380
    • Wang, Y.1    Huang, W.2    Sathitsuksanoh, N.3    Zhu, Z.4    Zhang, Y.-H.P.5
  • 375
    • 0036411713 scopus 로고    scopus 로고
    • The role of lymphatic transport in enhancing oral protein and peptide drug delivery
    • Wasan K.M. The role of lymphatic transport in enhancing oral protein and peptide drug delivery. Drug Dev Ind Pharm 2002, 28:1047-1058.
    • (2002) Drug Dev Ind Pharm , vol.28 , pp. 1047-1058
    • Wasan, K.M.1
  • 376
    • 0025482614 scopus 로고
    • Intestinal absorption of protein hydrolysis products: a review
    • Webb K.E. Intestinal absorption of protein hydrolysis products: a review. J Anim Sci 1990, 68:3011-3022.
    • (1990) J Anim Sci , vol.68 , pp. 3011-3022
    • Webb, K.E.1
  • 377
    • 77951598531 scopus 로고    scopus 로고
    • The Okinawan Diet: health implications of a low-calorie, nutrient-dense, antioxidant-rich dietary pattern low in glycemic load
    • Willcox D.C., Willcox B.J., Todoriki H., Suzuki M. The Okinawan Diet: health implications of a low-calorie, nutrient-dense, antioxidant-rich dietary pattern low in glycemic load. J Am Coll Nutr 2009, 28(4):500S-516S.
    • (2009) J Am Coll Nutr , vol.28 , Issue.4 , pp. 500S-516S
    • Willcox, D.C.1    Willcox, B.J.2    Todoriki, H.3    Suzuki, M.4
  • 379
    • 79959969840 scopus 로고    scopus 로고
    • Angiotensin-I-converting enzyme and prolyl endopeptidase inhibitory peptides from natural sources with a focus on marine processing by-products
    • Wilson J., Hayes M., Carney B. Angiotensin-I-converting enzyme and prolyl endopeptidase inhibitory peptides from natural sources with a focus on marine processing by-products. Food Chem 2011, 129:235-244.
    • (2011) Food Chem , vol.129 , pp. 235-244
    • Wilson, J.1    Hayes, M.2    Carney, B.3
  • 380
    • 25144465426 scopus 로고    scopus 로고
    • N-PEP-12 - a novel peptide compound that protects cortical neurons in culture against different age and disease associated lesions
    • Windisch M., Hutter-Paier B., Grygar E., Doppler E., Moessler H. N-PEP-12 - a novel peptide compound that protects cortical neurons in culture against different age and disease associated lesions. J Neural Transm 2005, 112:1331-1343.
    • (2005) J Neural Transm , vol.112 , pp. 1331-1343
    • Windisch, M.1    Hutter-Paier, B.2    Grygar, E.3    Doppler, E.4    Moessler, H.5
  • 382
    • 36148987289 scopus 로고    scopus 로고
    • Cellular antioxidant activity (CAA) assay for assessing antioxidants, foods, and dietary supplements
    • Wolfe K.L., Liu R.H. Cellular antioxidant activity (CAA) assay for assessing antioxidants, foods, and dietary supplements. J Agric Food Chem 2007, 55(22):8896-8907.
    • (2007) J Agric Food Chem , vol.55 , Issue.22 , pp. 8896-8907
    • Wolfe, K.L.1    Liu, R.H.2
  • 383
    • 43649098961 scopus 로고    scopus 로고
    • New opportunities for biocatalysis: making pharmaceutical processes greener
    • Woodley J.M. New opportunities for biocatalysis: making pharmaceutical processes greener. Trends Biotechnol 2008, 26:321-327.
    • (2008) Trends Biotechnol , vol.26 , pp. 321-327
    • Woodley, J.M.1
  • 385
    • 10744230552 scopus 로고    scopus 로고
    • Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus)
    • Wu C.H., Chen H.M., Shiau C.Y. Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus). Food Res Int 2003, 36:949-957.
    • (2003) Food Res Int , vol.36 , pp. 949-957
    • Wu, C.H.1    Chen, H.M.2    Shiau, C.Y.3
  • 386
    • 40649103346 scopus 로고    scopus 로고
    • Purification and identification of novel angiotensin-I-converting enzyme inhibitory peptides from shark meat hydrolysate
    • Wu H., He H.L., Chen X.L., Sun C.Y., Zhang Y.Z., Zhou B.C. Purification and identification of novel angiotensin-I-converting enzyme inhibitory peptides from shark meat hydrolysate. Process Biochem 2008, 43:457-461.
    • (2008) Process Biochem , vol.43 , pp. 457-461
    • Wu, H.1    He, H.L.2    Chen, X.L.3    Sun, C.Y.4    Zhang, Y.Z.5    Zhou, B.C.6
  • 387
    • 46949100238 scopus 로고    scopus 로고
    • Purification of angiotensin I-converting enzyme-inhibitory peptides from the enzymatic hydrolysate of defatted canola meal
    • Wu J., Aluko R.E., Muir A.D. Purification of angiotensin I-converting enzyme-inhibitory peptides from the enzymatic hydrolysate of defatted canola meal. Food Chem 2008, 111:942-950.
    • (2008) Food Chem , vol.111 , pp. 942-950
    • Wu, J.1    Aluko, R.E.2    Muir, A.D.3
  • 388
    • 51749125669 scopus 로고    scopus 로고
    • Antioxidant activity of peptides isolated from alfalfa leaf protein hydrolysate
    • Xie Z., Huang J., Xu X., Jin Z. Antioxidant activity of peptides isolated from alfalfa leaf protein hydrolysate. Food Chem 2008, 111:370-376.
    • (2008) Food Chem , vol.111 , pp. 370-376
    • Xie, Z.1    Huang, J.2    Xu, X.3    Jin, Z.4
  • 389
    • 0030873439 scopus 로고    scopus 로고
    • Antihypertensive peptides derived from food proteins
    • Yamamoto N. Antihypertensive peptides derived from food proteins. Biopolymers 1997, 43:129-134.
    • (1997) Biopolymers , vol.43 , pp. 129-134
    • Yamamoto, N.1
  • 390
    • 0028414339 scopus 로고
    • Antihypertensive effect of the peptides derived from casein by an extracellular proteinase from Lactobacillus helveticus CP790
    • Yamamoto N., Akino A., Takano T. Antihypertensive effect of the peptides derived from casein by an extracellular proteinase from Lactobacillus helveticus CP790. J Dairy Sci 1994, 77:917.
    • (1994) J Dairy Sci , vol.77 , pp. 917
    • Yamamoto, N.1    Akino, A.2    Takano, T.3
  • 391
    • 0032853619 scopus 로고    scopus 로고
    • Intestinal peptide transport systems and oral drug availability
    • Yang C.Y., Dantzig A.H., Pidgeon C. Intestinal peptide transport systems and oral drug availability. Pharm Res 1999, 16:1331-1343.
    • (1999) Pharm Res , vol.16 , pp. 1331-1343
    • Yang, C.Y.1    Dantzig, A.H.2    Pidgeon, C.3
  • 392
    • 7444269711 scopus 로고    scopus 로고
    • Functional properties of fractionated soy protein isolates by proteases from Meju
    • Yim M.H., Lee J.H. Functional properties of fractionated soy protein isolates by proteases from Meju. Food Sci Biotechnol 2000, 9:253-257.
    • (2000) Food Sci Biotechnol , vol.9 , pp. 253-257
    • Yim, M.H.1    Lee, J.H.2
  • 393
    • 0026936217 scopus 로고
    • Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito
    • Yokoyama K., Chiba H., Yoshikawa M. Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito. Biosci Biotechnol Biochem 1992, 56:1541-1545.
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 1541-1545
    • Yokoyama, K.1    Chiba, H.2    Yoshikawa, M.3
  • 394
    • 0031589527 scopus 로고    scopus 로고
    • Apoptosis in human leukemic cells induced by lactoferricin, a bovine milk protein-derived peptide: involvement of reactive oxygen species
    • Yoo Y.C., Watanabe R., Koike Y., Mitobe M., Shimazaki K., Watanabe S., et al. Apoptosis in human leukemic cells induced by lactoferricin, a bovine milk protein-derived peptide: involvement of reactive oxygen species. Biochem Biophys Res Commun 1997, 237(3):624-628.
    • (1997) Biochem Biophys Res Commun , vol.237 , Issue.3 , pp. 624-628
    • Yoo, Y.C.1    Watanabe, R.2    Koike, Y.3    Mitobe, M.4    Shimazaki, K.5    Watanabe, S.6
  • 396
    • 79961128366 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme (ACE) inhibitory and antioxidant activities of egg protein hydrolysates produced with gastrointestinal and nongastrointestinal enzymes
    • You S.J., Wu J. Angiotensin I converting enzyme (ACE) inhibitory and antioxidant activities of egg protein hydrolysates produced with gastrointestinal and nongastrointestinal enzymes. J Food Sci 2011, 76:801-807.
    • (2011) J Food Sci , vol.76 , pp. 801-807
    • You, S.J.1    Wu, J.2
  • 397
    • 77953132207 scopus 로고    scopus 로고
    • Purification and identification of antioxidative peptides from loach (Misgurnus anguillicaudatus) protein hydrolysate by consecutive chromatography and electrospray ionization-mass spectrometry
    • You L., Zhao M., Regenstein J.M., Ren J. Purification and identification of antioxidative peptides from loach (Misgurnus anguillicaudatus) protein hydrolysate by consecutive chromatography and electrospray ionization-mass spectrometry. Food Res Int 2010, 43:1167-1173.
    • (2010) Food Res Int , vol.43 , pp. 1167-1173
    • You, L.1    Zhao, M.2    Regenstein, J.M.3    Ren, J.4
  • 398
    • 77955272203 scopus 로고    scopus 로고
    • In vitro antioxidant activity and in vivo anti-fatigue effect of loach (Misgurnus anguillicaudatus) peptides prepared by papain digestion
    • You L., Zhao M., Regenstein J.M., Ren J. In vitro antioxidant activity and in vivo anti-fatigue effect of loach (Misgurnus anguillicaudatus) peptides prepared by papain digestion. Food Chem 2011, 124(1):188-194.
    • (2011) Food Chem , vol.124 , Issue.1 , pp. 188-194
    • You, L.1    Zhao, M.2    Regenstein, J.M.3    Ren, J.4
  • 400
    • 0026321423 scopus 로고
    • Confirmation of calcuim absorption and femoral utilization in spontanously hypertensive rats fed casein phosphopeptide supplemented diets
    • Yuan Y.V., Kitts D.D. Confirmation of calcuim absorption and femoral utilization in spontanously hypertensive rats fed casein phosphopeptide supplemented diets. Nutr Res 1991, 11(11):1257-1272.
    • (1991) Nutr Res , vol.11 , Issue.11 , pp. 1257-1272
    • Yuan, Y.V.1    Kitts, D.D.2
  • 401
    • 51749125710 scopus 로고    scopus 로고
    • Purification and characterisation of a hypoglycemic peptide from Momordica charantia L. Var. abbreviata Ser
    • Yuan X., Gu X., Tang J. Purification and characterisation of a hypoglycemic peptide from Momordica charantia L. Var. abbreviata Ser. Food Chem 2008, 111:415-420.
    • (2008) Food Chem , vol.111 , pp. 415-420
    • Yuan, X.1    Gu, X.2    Tang, J.3
  • 402
    • 0037409169 scopus 로고    scopus 로고
    • Production of ace inhibitory peptides by digestion of chickpea legumin with alcalase
    • Yust M.M., Pedroche J., Calle J.G., Alaiz M., Millán F., Vioque J. Production of ace inhibitory peptides by digestion of chickpea legumin with alcalase. Food Chem 2003, 81:363-369.
    • (2003) Food Chem , vol.81 , pp. 363-369
    • Yust, M.M.1    Pedroche, J.2    Calle, J.G.3    Alaiz, M.4    Millán, F.5    Vioque, J.6
  • 404
    • 65749118184 scopus 로고    scopus 로고
    • A sweet out-of-the-box solution to the hydrogen economy: is the sugarpowered car science fiction?
    • Zhang Y.-H.P. A sweet out-of-the-box solution to the hydrogen economy: is the sugarpowered car science fiction?. Energy Environ Sci 2009, 2:272-282.
    • (2009) Energy Environ Sci , vol.2 , pp. 272-282
    • Zhang, Y.-H.P.1
  • 405
    • 77449142867 scopus 로고    scopus 로고
    • Production of biocommodities and bioelectricity by cell-free synthetic enzymatic pathway biotransformations: challenges and opportunities
    • Zhang Y.-H.P. Production of biocommodities and bioelectricity by cell-free synthetic enzymatic pathway biotransformations: challenges and opportunities. Biotechnol Bioeng 2010, 105:663-677.
    • (2010) Biotechnol Bioeng , vol.105 , pp. 663-677
    • Zhang, Y.-H.P.1
  • 406
    • 77957256912 scopus 로고    scopus 로고
    • Renewable carbohydrates are a potential high density hydrogen carrier
    • Zhang Y.-H.P. Renewable carbohydrates are a potential high density hydrogen carrier. Int J Hydrogen Energy 2010, 35:10334-10342.
    • (2010) Int J Hydrogen Energy , vol.35 , pp. 10334-10342
    • Zhang, Y.-H.P.1
  • 407
    • 79960216783 scopus 로고    scopus 로고
    • Substrate channeling and enzyme complexes for biotechnological applications
    • Zhang Y.-H.P. Substrate channeling and enzyme complexes for biotechnological applications. Biotechnol Adv 2011, 29:715-725.
    • (2011) Biotechnol Adv , vol.29 , pp. 715-725
    • Zhang, Y.-H.P.1
  • 408
    • 33645803815 scopus 로고    scopus 로고
    • Antimicrobial peptides: therapeutic potential
    • Zhang L., Falla T.J. Antimicrobial peptides: therapeutic potential. Expert Opin Pharmacother 2006, 7(6):653-663.
    • (2006) Expert Opin Pharmacother , vol.7 , Issue.6 , pp. 653-663
    • Zhang, L.1    Falla, T.J.2
  • 409
    • 22944460826 scopus 로고    scopus 로고
    • Artificial polypeptide scaffold for protein immobilization
    • Zhang K., Diehl M.R., Tirrell D.A. Artificial polypeptide scaffold for protein immobilization. J Am Chem Soc 2005, 127:10136-10137.
    • (2005) J Am Chem Soc , vol.127 , pp. 10136-10137
    • Zhang, K.1    Diehl, M.R.2    Tirrell, D.A.3
  • 410
    • 33645232931 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides in douchi, a Chinese traditional fermented soybean product
    • Zhang J.-H., Tatsumi E., Ding C.-H., Li L.-T. Angiotensin I-converting enzyme inhibitory peptides in douchi, a Chinese traditional fermented soybean product. Food Chem 2006, 98:551-557.
    • (2006) Food Chem , vol.98 , pp. 551-557
    • Zhang, J.-H.1    Tatsumi, E.2    Ding, C.-H.3    Li, L.-T.4
  • 411
    • 70349816703 scopus 로고    scopus 로고
    • Isolation and identification of antioxidative peptide from rice endosperm protein enzymatic hydrolysate by consecutive chromatography and MALDI-TOF/TOF MS/MS
    • Zhang J., Zhang H., Wang L., Guo X., Wang X., Yao H. Isolation and identification of antioxidative peptide from rice endosperm protein enzymatic hydrolysate by consecutive chromatography and MALDI-TOF/TOF MS/MS. Food Chem 2010, 119:226-234.
    • (2010) Food Chem , vol.119 , pp. 226-234
    • Zhang, J.1    Zhang, H.2    Wang, L.3    Guo, X.4    Wang, X.5    Yao, H.6
  • 412
    • 79954421764 scopus 로고    scopus 로고
    • Purification and characterisation of a new antioxidant peptide from chickpea (Cicer arietium L.) protein hydrolysates
    • Zhang T., Li Y., Miao M., Jiang B. Purification and characterisation of a new antioxidant peptide from chickpea (Cicer arietium L.) protein hydrolysates. Food Chem 2011, 128:28-33.
    • (2011) Food Chem , vol.128 , pp. 28-33
    • Zhang, T.1    Li, Y.2    Miao, M.3    Jiang, B.4
  • 413
    • 84922884336 scopus 로고    scopus 로고
    • Mitochondriatargeted peptide prevents mitochondrial depolarization and apoptosis induced by tert-butyl hydroperoxide in neuronal cell monolayers
    • Zhao K., Luo G., Giannelli S., Szeto H.H. Mitochondriatargeted peptide prevents mitochondrial depolarization and apoptosis induced by tert-butyl hydroperoxide in neuronal cell monolayers. Biosci Biotechnol Biochem 2005, 6:378-384.
    • (2005) Biosci Biotechnol Biochem , vol.6 , pp. 378-384
    • Zhao, K.1    Luo, G.2    Giannelli, S.3    Szeto, H.H.4
  • 414
    • 67349231325 scopus 로고    scopus 로고
    • A novel ACE inhibitory peptide isolated from Acaudina molpadioidea hydrolysate
    • Zhao Y., Bafang L., Dong S., Liu Z., Zhao X., Wang J., et al. A novel ACE inhibitory peptide isolated from Acaudina molpadioidea hydrolysate. Peptides 2009, 30:1028-1033.
    • (2009) Peptides , vol.30 , pp. 1028-1033
    • Zhao, Y.1    Bafang, L.2    Dong, S.3    Liu, Z.4    Zhao, X.5    Wang, J.6
  • 415
    • 34247619388 scopus 로고    scopus 로고
    • Preparation of hypocholesterol peptides from soy protein and their hypocholesterolemic effect in mice
    • Zhong F., Liu J., Ma J., Shoemaker C.F. Preparation of hypocholesterol peptides from soy protein and their hypocholesterolemic effect in mice. Food Res Int 2007, 40:661-667.
    • (2007) Food Res Int , vol.40 , pp. 661-667
    • Zhong, F.1    Liu, J.2    Ma, J.3    Shoemaker, C.F.4
  • 416
    • 79551562904 scopus 로고    scopus 로고
    • Antioxidant properties of peptide fractions from silver carp (Hypophthalmichthys molitrix) processing by-product protein hydrolysates evaluated by spin resonance spectrometry
    • Zhong S., Ma C., Lin Y.C., Luo Y. Antioxidant properties of peptide fractions from silver carp (Hypophthalmichthys molitrix) processing by-product protein hydrolysates evaluated by spin resonance spectrometry. Food Chem 2011, 126(4):1636-1642.
    • (2011) Food Chem , vol.126 , Issue.4 , pp. 1636-1642
    • Zhong, S.1    Ma, C.2    Lin, Y.C.3    Luo, Y.4
  • 417
    • 0032819575 scopus 로고    scopus 로고
    • Ability of amino acids, dipeptides, polyamines, and sulfhydryls to quench hexanal, a saturated aldehydic lipid oxidation product
    • Zhou S., Decker E.A. Ability of amino acids, dipeptides, polyamines, and sulfhydryls to quench hexanal, a saturated aldehydic lipid oxidation product. J Agric Food Chem 1999, 47:1932-1936.
    • (1999) J Agric Food Chem , vol.47 , pp. 1932-1936
    • Zhou, S.1    Decker, E.A.2
  • 418
    • 33947363724 scopus 로고    scopus 로고
    • Milk-derived proteins and peptides of potential therapeutic and nutritive value
    • Zimecki M., Kruzel M.L. Milk-derived proteins and peptides of potential therapeutic and nutritive value. J Exp Ther Oncol 2007, 6:89-106.
    • (2007) J Exp Ther Oncol , vol.6 , pp. 89-106
    • Zimecki, M.1    Kruzel, M.L.2
  • 419
    • 0034657529 scopus 로고    scopus 로고
    • Intestinal absorption of peptides through the enterocytes
    • Ziv E., Bendayan M. Intestinal absorption of peptides through the enterocytes. Microsc Res Tech 2000, 49:346-352.
    • (2000) Microsc Res Tech , vol.49 , pp. 346-352
    • Ziv, E.1    Bendayan, M.2


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