메뉴 건너뛰기




Volumn 93, Issue 9, 2014, Pages 2347-2362

Low molecular weight bioactive peptides derived from the enzymatic hydrolysis of collagen after isoelectric solubilization/precipitation process of turkey by-products

Author keywords

Anti inflammatory peptide; Anticholesteremic peptide; Enzyme cocktail; Isoelectric solubilization precipitation; Turkey collagen

Indexed keywords

AVIAN PROTEIN; COLLAGEN; FLAVOURZYME; PEPTIDE; PROTEINASE; SUBTILISIN; TRYPSIN;

EID: 84906862102     PISSN: 00325791     EISSN: 15253171     Source Type: Journal    
DOI: 10.3382/ps.2014-03953     Document Type: Article
Times cited : (82)

References (59)
  • 2
    • 85012738381 scopus 로고
    • The estimation of pepsin, trypsin, papain, and cathepsin with hemoglobin. The estimation of pepsin, trypsin, papain, and cathepsin with hemoglobin
    • Anson, M. L. 1938. The estimation of pepsin, trypsin, papain, and cathepsin with hemoglobin. The estimation of pepsin, trypsin, papain, and cathepsin with hemoglobin. J. Gen. Physiol. 22: 79-89.
    • (1938) J. Gen. Physiol. , vol.22 , pp. 79-89
    • Anson, M.L.1
  • 3
    • 70349998626 scopus 로고    scopus 로고
    • Therapeutic application of peptides and proteins: Parenteral forever?
    • Antosova, Z., M. Mackova, V. Kral, and T. Macek. 2009. Therapeutic application of peptides and proteins: Parenteral forever? Trends Biotechnol. 27: 628-635.
    • (2009) Trends Biotechnol. , vol.27 , pp. 628-635
    • Antosova, Z.1    Mackova, M.2    Kral, V.3    Macek, T.4
  • 5
    • 84906869881 scopus 로고    scopus 로고
    • Process for making a low molecular weight gelatine hydrolysate and gelatine hydrolysate compositions. Gelita ag, assignee
    • No. 1885771
    • Babel, W., J. M. Dolphin, T. Keenan, and J. D. Russell. 2008. Process for making a low molecular weight gelatine hydrolysate and gelatine hydrolysate compositions. Gelita Ag, assignee. European Pat. No. 1885771.
    • (2008) European Pat.
    • Babel, W.1    Dolphin, J.M.2    Keenan, T.3    Russell, J.D.4
  • 6
    • 0037471605 scopus 로고    scopus 로고
    • Raisin dietary fiber composition and in vitro bile acid binding
    • Camire, M. E., and M. P. Dougherty. 2003. Raisin dietary fiber composition and in vitro bile acid binding. J. Agric. Food Chem. 51: 834-837.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 834-837
    • Camire, M.E.1    Dougherty, M.P.2
  • 8
    • 85022241054 scopus 로고
    • Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins
    • Church, F. C., H. E. Swaisgood, D. H. Porter, and G. L. Catignani. 1983. Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. J. Dairy Sci. 66: 1219-1227.
    • (1983) J. Dairy Sci. , vol.66 , pp. 1219-1227
    • Church, F.C.1    Swaisgood, H.E.2    Porter, D.H.3    Catignani, G.L.4
  • 9
    • 36448957177 scopus 로고    scopus 로고
    • Antioxidant and biochemical properties of protein hydrolysates prepared from silver carp (hypophthalmichthys molitrix
    • Dong, S., M. Zeng, D. Wang, Z. Liu, Y. Zao, and H. Yang. 2008. Antioxidant and biochemical properties of protein hydrolysates prepared from silver carp (Hypophthalmichthys molitrix). Food Chem. 107: 1485-1493.
    • (2008) Food Chem. , vol.107 , pp. 1485-1493
    • Dong, S.1    Zeng, M.2    Wang, D.3    Liu, Z.4    Zao, Y.5    Yang, H.6
  • 10
    • 84898035360 scopus 로고    scopus 로고
    • Preparation and characterization of gelatin from collagen biomass obtained through a ph-shifting process of mechanically separated turkey meat
    • Du, L., L. Keplová, Z. Khiari, and M. Betti. 2014. Preparation and characterization of gelatin from collagen biomass obtained through a pH-shifting process of mechanically separated turkey meat. Poult. Sci. 93: 989-1000.
    • (2014) Poult. Sci. , vol.93 , pp. 989-1000
    • Du, L.1    Keplová, L.2    Khiari, Z.3    Betti, M.4
  • 11
    • 84882647585 scopus 로고    scopus 로고
    • Physico-chemical and functional properties of gelatins extracted from turkey and chicken heads
    • Du, L., Z. Khiari, Z. Pietrasik, and M. Betti. 2013. Physico-chemical and functional properties of gelatins extracted from turkey and chicken heads. Poult. Sci. 92: 2463-2474.
    • (2013) Poult. Sci. , vol.92 , pp. 2463-2474
    • Du, L.1    Khiari, Z.2    Pietrasik, Z.3    Betti, M.4
  • 12
    • 0242695364 scopus 로고
    • A method for the determination of total nitrogen in proteins
    • Series B5. Nature Publishing Group, London, UK
    • Eastoe, J. E., and B. Eastoe. 1952. A method for the determination of total nitrogen in proteins. Pages 1-17 in The British Gelatin and Glue Research Association Research Report, Series B5. Nature Publishing Group, London, UK.
    • (1952) The British Gelatin and Glue Research Association Research Report , pp. 1-17
    • Eastoe, J.E.1    Eastoe, B.2
  • 13
    • 0018869798 scopus 로고
    • Modified assay for determination of hydroxyl-proline in a tissue hydrolyzate
    • Edwards, C. A., and W. D. O'Brien Jr.. 1980. Modified assay for determination of hydroxyl-proline in a tissue hydrolyzate. Clin. Chim. Acta 104: 161-167.
    • (1980) Clin. Chim. Acta , vol.104 , pp. 161-167
    • Edwards, C.A.1    O'Brien Jr., W.D.2
  • 14
    • 84906869882 scopus 로고    scopus 로고
    • The United States Pharmacopeial Convention, Rockville, MD
    • Food Chemicals Codex. 2012. Eighth edition. The United States Pharmacopeial Convention, Rockville, MD.
    • (2012) Eighth Edition
    • Codex, F.C.1
  • 15
    • 7444233676 scopus 로고    scopus 로고
    • Influence of hydrolysis degree on the functional properties of salmon byproduct hydrolysates
    • Gbogouri, G. A., M. Linder, J. Fanni, and M. Parmentier. 2004. Influence of hydrolysis degree on the functional properties of salmon byproduct hydrolysates. J. Food Sci. 69: 615-622.
    • (2004) J. Food Sci. , vol.69 , pp. 615-622
    • Gbogouri, G.A.1    Linder, M.2    Fanni, J.3    Parmentier, M.4
  • 16
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall, A. G., C. J. Bardawill, and M. M. David. 1949. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177: 751-766.
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 17
    • 84906849421 scopus 로고    scopus 로고
    • Gelatin
    • G. O. Phillips, and P. A. Williams, ed. Woodhead Publishing Ltd., Cambridge, UK
    • Haug, I. J., and K. I. Draget. 2011. Gelatin. Pages 92-115 in Handbook of Food Proteins. G. O. Phillips, and P. A. Williams, ed. Woodhead Publishing Ltd., Cambridge, UK.
    • (2011) Handbook of Food Proteins , pp. 92-115
    • Haug, I.J.1    Draget, K.I.2
  • 18
    • 84887232284 scopus 로고    scopus 로고
    • Biological activities of proteins and marine-derived peptides from byproducts and seaweeds
    • S. K. Kim, ed. John Wiley & Sons Ltd., Chichester, UK
    • Hayes, M. 2013. Biological activities of proteins and marine-derived peptides from byproducts and seaweeds. Pages 139-165 in Marine Proteins and Peptides: Biological Activities and Applications. S. K. Kim, ed. John Wiley & Sons Ltd., Chichester, UK.
    • (2013) Marine Proteins and Peptides: Biological Activities and Applications , pp. 139-165
    • Hayes, M.1
  • 20
    • 34250791622 scopus 로고    scopus 로고
    • A peroxidase-coupled continuous absorbance plate-reader assay for flavin monoamine oxidases, copper-containing amine oxidases and related enzymes
    • Holt, A., and M. M. Palcic. 2006. A peroxidase-coupled continuous absorbance plate-reader assay for flavin monoamine oxidases, copper-containing amine oxidases and related enzymes. Nat. Protoc. 1: 2498-2505.
    • (2006) Nat. Protoc. , vol.1 , pp. 2498-2505
    • Holt, A.1    Palcic, M.M.2
  • 21
    • 84881171951 scopus 로고    scopus 로고
    • Glycation and transglutaminase mediated glycosylation of fish gelatin peptides with glucosamine enhance bioactivity
    • Hong, P. K., D. Gottardi, M. Ndagijimana, and M. Betti. 2014. Glycation and transglutaminase mediated glycosylation of fish gelatin peptides with glucosamine enhance bioactivity. Food Chem. 142: 285-293.
    • (2014) Food Chem. , vol.142 , pp. 285-293
    • Hong, P.K.1    Gottardi, D.2    Ndagijimana, M.3    Betti, M.4
  • 22
    • 78650252283 scopus 로고    scopus 로고
    • Comparative study on the effect of acid-and alkaline-aided extractions on mechanically separated turkey meat (mstm): Chemical and functional properties of recovered proteins
    • Hrynets, Y., D. A. Omana, Y. Xu, and M. Betti. 2011. Comparative study on the effect of acid-and alkaline-aided extractions on Mechanically Separated Turkey Meat (MSTM): Chemical and functional properties of recovered proteins. Process Biochem. 46: 335-343.
    • (2011) Process Biochem. , vol.46 , pp. 335-343
    • Hrynets, Y.1    Omana, D.A.2    Xu, Y.3    Betti, M.4
  • 25
    • 0001568705 scopus 로고
    • Involvement of pot-digestion "hydrophobic" peptides in plasma cholesterol-lowering effect of dietary plant proteins
    • Iwami, K., K. Sakakibara, and F. Ibuki. 1986. Involvement of pot-digestion "hydrophobic" peptides in plasma cholesterol-lowering effect of dietary plant proteins. Agric. Biol. Chem. 50: 1217-1222.
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 1217-1222
    • Iwami, K.1    Sakakibara, K.2    Ibuki, F.3
  • 27
    • 0000145831 scopus 로고
    • Gelatin
    • P. Harris, ed. Elsevier Applied Science Publishers Ltd., London, UK
    • Johnston-Banks, F. A. 1990. Gelatin. Pages 233-289 in Food Gels. P. Harris, ed. Elsevier Applied Science Publishers Ltd., London, UK.
    • (1990) Food Gels , pp. 233-289
    • Johnston-Banks, F.A.1
  • 28
    • 84884922421 scopus 로고    scopus 로고
    • Gelatin
    • K. Matyjaszewski, and M. Möller, ed. Elsevier, Amsterdam, the Netherlands
    • Keenan, T. R. 2012. Gelatin. Pages 237-247 in Polymer Science: A Comprehensive Reference. K. Matyjaszewski, and M. Möller, ed. Elsevier, Amsterdam, the Netherlands.
    • (2012) Polymer Science: A Comprehensive Reference , pp. 237-247
    • Keenan, T.R.1
  • 31
    • 84875947686 scopus 로고    scopus 로고
    • Comparison between gelatines extracted from mackerel and blue whiting bones after different pre-treatments
    • Khiari, Z., D. Rico, A. B. Martin-Diana, and C. Barry-Ryan. 2013. Comparison between gelatines extracted from mackerel and blue whiting bones after different pre-treatments. Food Chem. 139: 347-354.
    • (2013) Food Chem. , vol.139 , pp. 347-354
    • Khiari, Z.1    Rico, D.2    Martin-Diana, A.B.3    Barry-Ryan, C.4
  • 32
    • 84900557961 scopus 로고    scopus 로고
    • Structure elucidation of ace-inhibitory and antithrombotic peptides isolated from mackerel skin gelatine hydrolysates
    • Khiari, Z., D. Rico, A. B. Martin-Diana, and C. Barry-Ryan. 2014. Structure elucidation of ACE-inhibitory and antithrombotic peptides isolated from mackerel skin gelatine hydrolysates. J. Sci. Food Agric. 94: 1663-1671. http://dx.doi.org/10.1002/jsfa.6476.
    • (2014) J. Sci. Food Agric. , vol.94 , pp. 1663-1671
    • Khiari, Z.1    Rico, D.2    Martin-Diana, A.B.3    Barry-Ryan, C.4
  • 33
    • 2942708160 scopus 로고    scopus 로고
    • A soybean kunitz trypsin inhibitor suppresses ovarian cancer cell invasion by blocking urokinase upregulation
    • Kobayashi, H., M. Suzuki, N. Kanayama, and T. Terao. 2004. A soybean Kunitz trypsin inhibitor suppresses ovarian cancer cell invasion by blocking urokinase upregulation. Clin. Exp. Metastasis 21: 159-166.
    • (2004) Clin. Exp. Metastasis , vol.21 , pp. 159-166
    • Kobayashi, H.1    Suzuki, M.2    Kanayama, N.3    Terao, T.4
  • 34
    • 79952257181 scopus 로고    scopus 로고
    • In vitro binding capacity of bile acids by defatted corn protein hydrolysate
    • Kongo-Dia-Moukala, J. U., H. Zhang, and P. C. Irakoze. 2011. In vitro binding capacity of bile acids by defatted corn protein hydrolysate. Int. J. Mol. Sci. 12: 1066-1080.
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 1066-1080
    • Kongo-Dia-Moukala, J.U.1    Zhang, H.2    Irakoze, P.C.3
  • 38
    • 6944241742 scopus 로고    scopus 로고
    • Release of short and proline-rich antihypertensive peptides from casein hydrolysate with an aspergillus oryzae protease
    • Mizuno, S., S. Nishimura, K. Matsuura, T. Gotou, and N. Yamamoto. 2004. Release of short and proline-rich antihypertensive peptides from casein hydrolysate with an Aspergillus oryzae protease. J. Dairy Sci. 87: 3183-3188.
    • (2004) J. Dairy Sci. , vol.87 , pp. 3183-3188
    • Mizuno, S.1    Nishimura, S.2    Matsuura, K.3    Gotou, T.4    Yamamoto, N.5
  • 39
    • 0033788841 scopus 로고    scopus 로고
    • Role of collagen hydrolysate in bone and joint disease
    • Moskowitz, R. W. 2000. Role of collagen hydrolysate in bone and joint disease. Semin. Arthritis Rheum. 30: 87-99.
    • (2000) Semin. Arthritis Rheum. , vol.30 , pp. 87-99
    • Moskowitz, R.W.1
  • 40
    • 84887216344 scopus 로고    scopus 로고
    • Cholesterol-lowering proteins and peptides
    • Y. Mine, and F. Shahidi, ed. CRC Press, Boca Raton, FL
    • Nagaoka, S. 2005. Cholesterol-lowering proteins and peptides. Pages 41-67 in Nutraceutical Proteins and Peptides in Health and Disease. Y. Mine, and F. Shahidi, ed. CRC Press, Boca Raton, FL.
    • (2005) Nutraceutical Proteins and Peptides in Health and Disease , pp. 41-67
    • Nagaoka, S.1
  • 43
    • 34250889578 scopus 로고    scopus 로고
    • L-lysine as a recognition molecule for the vap-1 function of ssao
    • Olivieri, A., K. Tipton, and J. O'Sullivan. 2007. L-lysine as a recognition molecule for the VAP-1 function of SSAO. J. Neural Transm. 114: 747-749.
    • (2007) J. Neural Transm. , vol.114 , pp. 747-749
    • Olivieri, A.1    Tipton, K.2    O'Sullivan, J.3
  • 45
    • 84878892982 scopus 로고    scopus 로고
    • Fungal cellulases and complexed cellulosomal enzymes exhibit synergistic mechanisms in cellulose deconstruction
    • Resch, M. G., B. S. Donohoe, J. O. Baker, S. R. Decker, E. A. Bayer, G. T. Beckham, and M. E. Himmel. 2013. Fungal cellulases and complexed cellulosomal enzymes exhibit synergistic mechanisms in cellulose deconstruction. Energy Environ. Sci. 6: 1858-1867.
    • (2013) Energy Environ. Sci. , vol.6 , pp. 1858-1867
    • Resch, M.G.1    Donohoe, B.S.2    Baker, J.O.3    Decker, S.R.4    Bayer, E.A.5    Beckham, G.T.6    Himmel, M.E.7
  • 47
    • 77956688199 scopus 로고    scopus 로고
    • Antioxidative peptides from food proteins: A review
    • Sarmadi, B. H., and A. Ismail. 2010. Antioxidative peptides from food proteins: A review. Peptides 31: 1949-1956.
    • (2010) Peptides , vol.31 , pp. 1949-1956
    • Sarmadi, B.H.1    Ismail, A.2
  • 48
    • 0003067652 scopus 로고    scopus 로고
    • A macro for converting mean separation output to letter groupings in Proc Mixed
    • SAS Institute, Cary, NC
    • Saxton, A. M. 1998. A macro for converting mean separation output to letter groupings in Proc Mixed. Pages 1243-1246 in Proc. 23rd SAS Users Group Int., SAS Institute, Cary, NC.
    • (1998) Proc. 23rd SAS Users Group Int. , pp. 1243-1246
    • Saxton, A.M.1
  • 50
    • 0017098645 scopus 로고
    • Comparisons of binding of various bile acids and bile salts in vitro by several types of fiber
    • Story, J. A., and D. Kritchevsky. 1976. Comparisons of binding of various bile acids and bile salts in vitro by several types of fiber. J. Nutr. 106: 1292-1294.
    • (1976) J. Nutr. , vol.106 , pp. 1292-1294
    • Story, J.A.1    Kritchevsky, D.2
  • 51
    • 84874702796 scopus 로고    scopus 로고
    • Reconstitution of a thermostable xylandegrading enzyme mixture from the bacterium caldicellulosiruptor bescii
    • Su, X., Y. Han, D. Dodd, Y. H. Moon, S. Yoshida, R. I. Mackie, and I. K. O. Cann. 2013. Reconstitution of a thermostable xylandegrading enzyme mixture from the bacterium Caldicellulosiruptor bescii. Appl. Environ. Microbiol. 79: 1481-1490.
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 1481-1490
    • Su, X.1    Han, Y.2    Dodd, D.3    Moon, Y.H.4    Yoshida, S.5    Mackie, R.I.6    Cann, I.K.O.7
  • 52
    • 64549113397 scopus 로고    scopus 로고
    • Flaxseed protein-derived peptide fractions: Antioxidant properties and inhibition of lipopolysaccharide-induced nitric oxide production in murine macrophages
    • Udenigwe, C. C., Y. L. Lu, C. H. Han, W. C. Hou, and R. E. Aluko. 2009. Flaxseed protein-derived peptide fractions: Antioxidant properties and inhibition of lipopolysaccharide-induced nitric oxide production in murine macrophages. Food Chem. 116: 277-284.
    • (2009) Food Chem. , vol.116 , pp. 277-284
    • Udenigwe, C.C.1    Lu, Y.L.2    Han, C.H.3    Hou, W.C.4    Aluko, R.E.5
  • 53
    • 84913545110 scopus 로고    scopus 로고
    • Prospects of functional foods/nutraceuticals and markets
    • K. G. Ramawat, and J. M. Mérillon, ed. Springer-Verlag, Berlin, Germany
    • Valls, J., N. Pasamontes, A. Pantaleón, S. Vinaixa, M. Vaqué, A. Soler, S. Millán, and X. Gómez. 2013. Prospects of Functional Foods/Nutraceuticals and Markets. Pages 2491-2525 in Natural Products. K. G. Ramawat, and J. M. Mérillon, ed. Springer-Verlag, Berlin, Germany.
    • (2013) Natural Products , pp. 2491-2525
    • Valls, J.1    Pasamontes, N.2    Pantaleón, A.3    Vinaixa, S.4    Vaqué, M.5    Soler, A.6    Millán, S.7    Gómez, X.8
  • 54
    • 84875914749 scopus 로고    scopus 로고
    • Chemical, rheological and surface morphologic characterization of spent hen proteins extracted by ph-shift processing with or without the presence of cryoprotectants
    • Wang, H., J. Wu, and M. Betti. 2013. Chemical, rheological and surface morphologic characterization of spent hen proteins extracted by pH-shift processing with or without the presence of cryoprotectants. Food Chem. 139: 710-719.
    • (2013) Food Chem. , vol.139 , pp. 710-719
    • Wang, H.1    Wu, J.2    Betti, M.3
  • 55
    • 84877266601 scopus 로고    scopus 로고
    • Regulation of nf-binduced inflammatory signaling by lipid peroxidation-derived aldehydes
    • Yadav, U. C. S., and K. V. Ramana. 2013. Regulation of NF-Binduced inflammatory signaling by lipid peroxidation-derived aldehydes. Oxid. Med. Cell. Longev. 2013: 690545.
    • (2013) Oxid. Med. Cell. Longev. , vol.2013 , pp. 690545
    • Yadav, U.C.S.1    Ramana, K.V.2
  • 56
    • 4444320761 scopus 로고    scopus 로고
    • A peptide inhibitor of vascular adhesion protein-1 (vap-1) blocks leukocyte-endothelium interactions under shear stress
    • Yegutkin, G. G., T. Salminen, K. Koskinen, C. Kurtis, M. J. McPherson, S. Jalkanen, and M. Salmi. 2004. A peptide inhibitor of vascular adhesion protein-1 (VAP-1) blocks leukocyte-endothelium interactions under shear stress. Eur. J. Immunol. 34: 2276-2285.
    • (2004) Eur. J. Immunol. , vol.34 , pp. 2276-2285
    • Yegutkin, G.G.1    Salminen, T.2    Koskinen, K.3    Kurtis, C.4    McPherson, M.J.5    Jalkanen, S.6    Salmi, M.7
  • 57
    • 3042701362 scopus 로고    scopus 로고
    • In vitro binding of bile acids by lupin protein isolates and their hydrolysates
    • Yoshie-Stark, Y., and A. Wäsche. 2004. In vitro binding of bile acids by lupin protein isolates and their hydrolysates. Food Chem. 88: 179-184.
    • (2004) Food Chem. , vol.88 , pp. 179-184
    • Yoshie-Stark, Y.1    Wäsche, A.2
  • 58
    • 34247619388 scopus 로고    scopus 로고
    • Preparation of hypocholesterol peptides from soy protein and their hypocholesterolemic effect in mice
    • Zhong, F., J. Liu, J. Ma, and C. F. Shoemaker. 2006. Preparation of hypocholesterol peptides from soy protein and their hypocholesterolemic effect in mice. Food Res. Int. 40: 661-667.
    • (2006) Food Res. Int. , vol.40 , pp. 661-667
    • Zhong, F.1    Liu, J.2    Ma, J.3    Shoemaker, C.F.4
  • 59
    • 34247641723 scopus 로고    scopus 로고
    • Fractionation and identification of a novel hypocholesterolemic peptide derived from soy protein alcalase hydrolysates
    • Zhong, F., X. Zhang, J. Ma, and C. F. Shoemaker. 2007. Fractionation and identification of a novel hypocholesterolemic peptide derived from soy protein Alcalase hydrolysates. Food Res. Int. 40: 756-762.
    • (2007) Food Res. Int. , vol.40 , pp. 756-762
    • Zhong, F.1    Zhang, X.2    Ma, J.3    Shoemaker, C.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.