메뉴 건너뛰기




Volumn 90, Issue 12, 2010, Pages 2006-2014

Influence of degree of hydrolysis on functional properties and angiotensin I-converting enzyme-inhibitory activity of protein hydrolysates from cuttlefish (Sepia officinalis) by-products

Author keywords

Angiotensin I converting enzyme inhibitor; Cuttlefish by product hydrolysates; Enzymatic hydrolysis; Functional properties; Sepia officinalis

Indexed keywords

ALKALINE PROTEINASE; ANGIOTENSIN I; BACTERIAL PROTEIN; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; FAT; FISH PROTEIN; PROTEIN HYDROLYSATE; PROTEINASE;

EID: 77955977361     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.4045     Document Type: Article
Times cited : (82)

References (70)
  • 1
    • 0019528715 scopus 로고
    • Nutritional value of fish viscera silage
    • Ström T and Eggum BO, Nutritional value of fish viscera silage. J Sci ood Agric 32:115-120 (1981).
    • (1981) J Sci Ood Agric , vol.32 , pp. 115-120
    • Ström, T.1    Eggum, B.O.2
  • 3
    • 0001797666 scopus 로고
    • Sea food processing by-products
    • ed. by Shahidi F and Botta JR. lackie Academic and Professional, London
    • Shahidi F, Sea food processing by-products, in Seafoods: Chemistry, rocessing Technology and Quality, ed. by Shahidi F and Botta JR. lackie Academic and Professional, London, pp. 321-334 (1994).
    • (1994) Seafoods: Chemistry, Rocessing Technology and Quality , pp. 321-334
    • Shahidi, F.1
  • 4
    • 0030127886 scopus 로고    scopus 로고
    • Enhancing thefunctionality of foodproteins by nzymaticmodification
    • Panyam DandKilara A, Enhancing thefunctionalityof foodproteins by nzymaticmodification. Trends Food Sci Technol 7:120-125 (1996).
    • (1996) Trends Food Sci Technol , vol.7 , pp. 120-125
    • Panyam, D.1    Kilara, A.2
  • 5
    • 0001947371 scopus 로고
    • Functional properties of fish protein hydrolysates
    • ed. by Hall GM. Blackie cademic and Professional, New York, NY
    • Hall GM and Ahmad NH, Functional properties of fish protein hydrolysates, in Fish Processing Technology, ed. by Hall GM. Blackie cademic and Professional, New York, NY, pp. 249-265 (1992).
    • (1992) Fish Processing Technology , pp. 249-265
    • Hall, G.M.1    Ahmad, N.H.2
  • 6
    • 7444234213 scopus 로고    scopus 로고
    • Purification and characterization f an antioxidative peptide from enzymatic hydrolysate of yellowfin ole (Limanda aspera) frame protein
    • Jun SY, Park PJ, Jung WK and Kim SK, Purification and characterization f an antioxidative peptide from enzymatic hydrolysate of yellowfin ole (Limanda aspera) frame protein. Eur Food Res Technol 19:20-26 (2004).
    • (2004) Eur Food Res Technol , vol.19 , pp. 20-26
    • Jun, S.Y.1    Park, P.J.2    Jung, W.K.3    Kim, S.K.4
  • 7
    • 7444222906 scopus 로고    scopus 로고
    • Antioxidant activity of a peptide isolated from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate
    • Je JY, Park PJ and Kim SK, Antioxidant activity of a peptide isolated from Alaska pollack (Theragra chalcogramma) frame protein hydrolysate. Food Res Int 38:45-50 (2005).
    • (2005) Food Res Int , vol.38 , pp. 45-50
    • Je, J.Y.1    Park, P.J.2    Kim, S.K.3
  • 8
    • 60249083915 scopus 로고    scopus 로고
    • Antioxidant and free radical-scavenging activities of smooth hound Mustelus mustelus) muscle protein hydrolysates obtained by astrointestinal proteases
    • Bougatef A, Hajji M, Balti R, Lassoued I, Triki-Ellouz Y and Nasri M, Antioxidant and free radical-scavenging activities of smooth hound Mustelus mustelus) muscle protein hydrolysates obtained by astrointestinal proteases. Food Chem 114:1198-1205 (2009).
    • (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
  • 9
    • 69349093252 scopus 로고    scopus 로고
    • Purification and identification of novel ntioxidant peptides from enzymatic hydrolysates of sardinelle Sardinella aurita) by-products proteins
    • BougatefA, Nedjar-ArroumeN, ManniL, RavallecR, BarkiaA, Guillochon D, et al, Purification and identification of novel ntioxidant peptides from enzymatic hydrolysates of sardinelle Sardinella aurita) by-products proteins. Food Chem 118:559-565 2010).
    • (2010) Food Chem , vol.118 , pp. 559-565
    • Bougatef, A.1    Nedjar-Arroume, N.2    Manni, L.3    Ravallec, R.4    Barkia, A.5    Guillochon, D.6
  • 10
    • 12344308529 scopus 로고    scopus 로고
    • Purification and identification of angiotensin onverting enzyme inhibitory peptides from beef hydrolysates
    • Jang A and Lee M, Purification and identification of angiotensin onverting enzyme inhibitory peptides from beef hydrolysates. eat Sci 69:653-661 (2005).
    • (2005) Eat Sci , vol.69 , pp. 653-661
    • Jang, A.1    Lee, M.2
  • 11
    • 51749125623 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme (ACE) inhibitory ctivities of sardinelle (Sardinella aurita) by-products protein ydrolysates obtained by treatment with microbial and visceral fish serine-proteases
    • Bougatef A, Nedjar-Arroume N, Ravallec-Plé R, Leroy Y, Guillochon D, Barkia A, et al, Angiotensin I-converting enzyme (ACE) inhibitory ctivities of sardinelle (Sardinella aurita) by-products protein ydrolysates obtained by treatment with microbial and visceral fish serine-proteases. Food Chem 111:350-356 (2008).
    • (2008) Food Chem , vol.111 , pp. 350-356
    • Bougatef, A.1    Nedjar-Arroume, N.2    Ravallec-Plé, R.3    Leroy, Y.4    Guillochon, D.5    Barkia, A.6
  • 12
    • 77952502725 scopus 로고    scopus 로고
    • Evaluation of angiotensin-I converting enzyme ACE) inhibitory activities of smooth hound (Mustelus mustelus) uscle protein hydrolysates generated by gastrointestinal roteases: Identification of the most potent active peptide
    • Bougatef A, Balti R, Nedjar-Arroume N, Ravallec R, Yaba Adjé E, Lassoued I, et al, Evaluation of angiotensin-I converting enzyme ACE) inhibitory activities of smooth hound (Mustelus mustelus) uscle protein hydrolysates generated by gastrointestinal roteases: identification of the most potent active peptide. Eur ood Res Technol 231:127-135 (2010).
    • (2010) Eur Ood Res Technol , vol.231 , pp. 127-135
    • Bougatef, A.1    Balti, R.2    Nedjar-Arroume, N.3    Ravallec, R.4    Yaba Adjé, E.5    Lassoued, I.6
  • 13
    • 77953135393 scopus 로고    scopus 로고
    • Three novel angiotensin I-converting enzyme (ACE) inhibitory eptides fromcuttlefish (Sepia officinalis) using digestive proteases
    • Balti R, Nedjar-Arroume N, Bougatef A, Guillochon D and Nasri M, Three novel angiotensin I-converting enzyme (ACE) inhibitory eptides fromcuttlefish (Sepia officinalis) using digestive proteases. Food Res Int 43:1136-1143 (2010).
    • (2010) Food Res Int , vol.43 , pp. 1136-1143
    • Balti, R.1    Nedjar-Arroume, N.2    Bougatef, A.3    Guillochon, D.4    Nasri, M.5
  • 14
    • 77949802114 scopus 로고    scopus 로고
    • Analysis of novel angiotensin I-converting enzyme inhibitory eptides from enzymatic hydrolysates of cuttlefish (Sepiaofficinalis) uscle proteins
    • Balti R, Nedjar-Arroume N, Yaba Adjé E, Guillochon D and Nasri M, Analysis of novel angiotensin I-converting enzyme inhibitory eptides from enzymatic hydrolysates of cuttlefish (Sepiaofficinalis) uscle proteins. J Agric Food Chem 58:3840-3846 (2010).
    • (2010) J Agric Food Chem , vol.58 , pp. 3840-3846
    • Balti, R.1    Nedjar-Arroume, N.2    Yaba Adjé, E.3    Guillochon, D.4    Nasri, M.5
  • 15
    • 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 4:139-144 (1993).
    • (1993) Trends Food Sci Technol , vol.4 , pp. 139-144
    • Ariyoshi, Y.1
  • 16
    • 33847265270 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of a detergent stable alkaline serine-protease from a newly isolated acillus licheniformis NH1
    • El Hadj-Ali N, Agrebi R, Ghorbel-Frikha B, Sellami-Kamoun A, Kanoun S and Nasri M, Biochemical and molecular characterization of a detergent stable alkaline serine-protease from a newly isolated acillus licheniformis NH1. Enzyme Microb Technol 40:513-523 (2007).
    • (2007) Enzyme Microb Technol , vol.40 , pp. 513-523
    • El Hadj-Ali, N.1    Agrebi, R.2    Ghorbel-Frikha, B.3    Sellami-Kamoun, A.4    Nasri, M.5
  • 17
    • 0027352759 scopus 로고
    • Salt-tolerant and thermostable lkaline protease from Bacillus subtilis NCIM No. 64
    • Kembhavi AA, Kulkarni A and Pant A, Salt-tolerant and thermostable lkaline protease from Bacillus subtilis NCIM No. 64. Appl Biochem iotechnol 38:83-92 (1993).
    • (1993) Appl Biochem Iotechnol , vol.38 , pp. 83-92
    • Kembhavi, A.A.1    Kulkarni, A.2    Pant, A.3
  • 18
    • 0002494352 scopus 로고
    • A review of food hydrolysis specific areas
    • ed. by Adler-Nissen J. Elsevier Applied cience, Copenhagen
    • Adler-Nissen J, A review of food hydrolysis specific areas, in Enzymic ydrolysis of Food Proteins, ed. by Adler-Nissen J. Elsevier Applied cience, Copenhagen, pp. 57-109 (1986).
    • (1986) Enzymic Ydrolysis of Food Proteins , pp. 57-109
    • Adler-Nissen, J.1
  • 19
    • 0004202155 scopus 로고
    • AOAC, (16th edn). Association of Official nalytical Chemists, Arlington, VA
    • AOAC, Official Methods of Analysis (16th edn). Association of Official nalytical Chemists, Arlington, VA (1995).
    • (1995) Official Methods of Analysis
  • 21
    • 29744466425 scopus 로고
    • Determinations of serum roteins by means of the biuret reactions
    • Gornall AG, Bardawill CJ and David MM, Determinations of serum roteins by means of the biuret reactions. J Biol Chem177:751-767 (1949).
    • (1949) J Biol Chem , vol.177 , pp. 751-767
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 22
    • 0001221842 scopus 로고
    • A comparative study of the hipping potential of an extract from several oilseed flours
    • Lawhon JT, Cater CM and Mattil KF, A comparative study of the hipping potential of an extract from several oilseed flours. Cereal ci Today 17:240-246 (1972).
    • (1972) Cereal Ci Today , vol.17 , pp. 240-246
    • Lawhon, J.T.1    Cater, C.M.2    Mattil, K.F.3
  • 23
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: Valuation of a turbidimetric technique
    • Pearce KN and Kinsella JE, Emulsifying properties of proteins: valuation of a turbidimetric technique. J Agric Food Chem 6:716-723 (1978).
    • (1978) J Agric Food Chem , vol.6 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 24
    • 0029029764 scopus 로고
    • Production and characteristics f protein hydrolysates from capelin (Mallotus villosus)
    • Shahidi F, Han XQ and Synowiecki J, Production and characteristics f protein hydrolysates from capelin (Mallotus villosus). Food Chem 3:285-293 (1995).
    • (1995) Food Chem , vol.3 , pp. 285-293
    • Shahidi, F.1    Han, X.Q.2    Synowiecki, J.3
  • 25
    • 13844320199 scopus 로고    scopus 로고
    • Characteristics of rotein fractions generated from hydrolysed cod (Gadus morhua) y-products
    • Šližyte R, Daukšas E, Falch E, Storrø I and Rustad T, Characteristics of rotein fractions generated from hydrolysed cod (Gadus morhua) y-products. Process Biochem 40:2021-2033 (2005).
    • (2005) Process Biochem , vol.40 , pp. 2021-2033
    • Šližyte, R.1    Daukšas, E.2    Falch, E.3    Storrø, I.4    Rustad, T.5
  • 26
    • 84987299319 scopus 로고
    • Physicochemical and functional properties of inged bean flour and isolate compared with soy isolate
    • Okezie BO and Bello AB, Physicochemical and functional properties of inged bean flour and isolate compared with soy isolate. J Food Sci 3:450-454 (1988).
    • (1988) J Food Sci , vol.3 , pp. 450-454
    • Okezie, B.O.1    Bello, A.B.2
  • 27
    • 0029286291 scopus 로고
    • Purification and characterization of angiotensin Iconverting- nzyme inhibitors fromsour milk
    • Nakamura Y, Yamamoto N, Sakai K, Okubo A, Yamazaki S and Takano T, Purification and characterization of angiotensin Iconverting- nzyme inhibitors fromsour milk.JDairySci 78:777-783 (1995).
    • (1995) JDairySci , vol.78 , pp. 777-783
    • Nakamura, Y.1    Yamamoto, N.2    Sakai, K.3    Okubo, A.4    Yamazaki, S.5    Takano, T.6
  • 28
    • 84985386368 scopus 로고
    • Enzymic solubilization of proteins of sardine (Sardina pilchardus) by commercial proteases
    • Quaglia GB and Orban E, Enzymic solubilization of proteins of sardine (Sardina pilchardus) by commercial proteases. J Sci Food Agric 8:263-269 (1987).
    • (1987) J Sci Food Agric , vol.8 , pp. 263-269
    • Quaglia, G.B.1    Orban, E.2
  • 29
    • 0034117422 scopus 로고    scopus 로고
    • Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with arious alkaline proteases
    • Kristinsson HG and Rasco BA, Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with arious alkaline proteases. J Agric Food Chem 48:657-666 (2000).
    • (2000) J Agric Food Chem , vol.48 , pp. 657-666
    • Kristinsson, H.G.1    Rasco, B.A.2
  • 30
    • 0033372096 scopus 로고    scopus 로고
    • Functional properties of fish rotein hydrolysate from herring (Clupea harengus)
    • Liceaga-Gesualdo AM and Li-Chan ECY, Functional properties of fish rotein hydrolysate from herring (Clupea harengus). J Food Sci 4:1000-1004 (1999).
    • (1999) J Food Sci , vol.4 , pp. 1000-1004
    • Liceaga-Gesualdo, A.M.1    Li-Chan, E.C.Y.2
  • 31
    • 34547340444 scopus 로고    scopus 로고
    • Biochemical and functional properties of sardinella (Sardinella aurita) by-product ydrolysates
    • Souissi N, Bougatef A, Triki-Ellouz Y and Nasri M, Biochemical and functional properties of sardinella (Sardinella aurita) by-product ydrolysates. Food Technol Biotechnol 45:187-194 (2007).
    • (2007) Food Technol Biotechnol , vol.45 , pp. 187-194
    • Souissi, N.1    Bougatef, A.2    Triki-Ellouz, Y.3    Nasri, M.4
  • 32
    • 26844546698 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of cod (Gadus orhua) by-products. Optimization of yield and properties of lipid and protein fractions
    • Šližyte R, Rustad T and Storrø I, Enzymatic hydrolysis of cod (Gadus orhua) by-products. Optimization of yield and properties of lipid and protein fractions. Process Biochem 40:3680-3692 (2005).
    • (2005) Process Biochem , vol.40 , pp. 3680-3692
    • Šližyte, R.1    Rustad, T.2    Storrø, I.3
  • 33
    • 0001920529 scopus 로고
    • Enzymatic processing of marine raw-materials
    • Gildberg A, Enzymatic processing of marine raw-materials. Process iochem 28:1-15 (1993).
    • (1993) Process Iochem , vol.28 , pp. 1-15
    • Gildberg, A.1
  • 34
    • 0038773324 scopus 로고
    • Approaches to the utilisation of fish or the preparation of protein isolates; enzymic modifications of yofibrillar fish proteins
    • Spinelli J, Koury B and Miller R, Approaches to the utilisation of fish or the preparation of protein isolates; enzymic modifications of yofibrillar fish proteins. J Food Sci 37:604-608 (1972).
    • (1972) J Food Sci , vol.37 , pp. 604-608
    • Spinelli, J.1    Koury, B.2    Miller, R.3
  • 35
    • 18844397356 scopus 로고    scopus 로고
    • Optimization of nzymatic hydrolysis of fish soluble concentrate by commercial roteases
    • Suthasinee N, Sittiwat L, Manop S and Apinya A, Optimization of nzymatic hydrolysis of fish soluble concentrate by commercial roteases. J Food Eng 70:571-578 (2005).
    • (2005) J Food Eng , vol.70 , pp. 571-578
    • Suthasinee, N.1    Sittiwat, L.2    Manop, S.3    Apinya, A.4
  • 37
    • 0026314892 scopus 로고
    • Study of the efficiency f amobile phase used in size-exclusion HPLC for the separation of eptidesfromacaseinhydrolysate accordingtotheirhydrodynamic volume
    • Lemieux L, Piot JM, Guillochon D and Amiot J, Study of the efficiency f amobile phase used in size-exclusion HPLC for the separation of eptidesfromacaseinhydrolysate accordingtotheirhydrodynamic volume. Chromatographia 31:499-504 (1991).
    • (1991) Chromatographia , vol.31 , pp. 499-504
    • Lemieux, L.1    Piot, J.M.2    Guillochon, D.3    Amiot, J.4
  • 38
    • 84920780688 scopus 로고
    • Enzymatic hydrolysis of asein: Effect of degree of hydrolysis on antigenicity and physical roperties
    • Mahmoud MI, Malone WT and Cordle CT, Enzymatic hydrolysis of asein: effect of degree of hydrolysis on antigenicity and physical roperties. J Food Sci 57:1223-1229 (1992).
    • (1992) J Food Sci , vol.57 , pp. 1223-1229
    • Mahmoud, M.I.1    Malone, W.T.2    Cordle, C.T.3
  • 39
    • 0018412136 scopus 로고
    • Hydrophobic high-performance liquid hromatography of hormonal polypeptides and proteins on alkylsilane bonded silica
    • O'Hare MJ and Nice EC, Hydrophobic high-performance liquid hromatography of hormonal polypeptides and proteins on alkylsilane bonded silica. J Chromatogr 171:209-226 (1979).
    • (1979) J Chromatogr , vol.171 , pp. 209-226
    • O'Hare, M.J.1    Nice, E.C.2
  • 40
    • 33845280838 scopus 로고
    • Solubility and mulsifying properties of caseins and whey proteins modified enzymatically by trypsin
    • Chobert JM, Bertrand-Harb C and Nicolas MG, Solubility and mulsifying properties of caseins and whey proteins modified enzymatically by trypsin. J Agric Food Chem 36:883-892 (1988).
    • (1988) J Agric Food Chem , vol.36 , pp. 883-892
    • Chobert, J.M.1    Bertrand-Harb, C.2    Nicolas, M.G.3
  • 41
    • 0002968338 scopus 로고
    • Studies on the recovery of proteinaceous substances from chicken heads. I. An application of neutrase to the production of protein hydrolysate
    • Surowka K and Fik M, Studies on the recovery of proteinaceous substances from chicken heads. I. An application of neutrase to the production of protein hydrolysate. Int J Food Sci Technol 27:9-20 (1992).
    • (1992) Int J Food Sci Technol , vol.27 , pp. 9-20
    • Surowka, K.1    Fik, M.2
  • 42
    • 84985292797 scopus 로고
    • Mathematical model for formation rate and collapse of foams from enzyme modified wheat flours
    • Bombara N, Pilosof AMR and Añnón MC, Mathematical model for formation rate and collapse of foams from enzyme modified wheat flours. J Food Sci 59:626-630 (1994).
    • (1994) J Food Sci , vol.59 , pp. 626-630
    • Bombara, N.1    Pilosof, A.M.R.2    Añnón, M.C.3
  • 43
    • 33748323487 scopus 로고    scopus 로고
    • Enzymatic preparation and functional properties of wheat gluten hydrolysates
    • Kong X, Zhou H and Qian H, Enzymatic preparation and functional properties of wheat gluten hydrolysates. Food Chem 101:615-620 (2007).
    • (2007) Food Chem , vol.101 , pp. 615-620
    • Kong, X.1    Zhou, H.2    Qian, H.3
  • 44
    • 0000997716 scopus 로고
    • Modification of functional properties of soy proteins by proteolytic enzyme treatment
    • Puski G, Modification of functional properties of soy proteins by proteolytic enzyme treatment. Cereal Chem 52:655-664 (1975).
    • (1975) Cereal Chem , vol.52 , pp. 655-664
    • Puski, G.1
  • 45
    • 0017528647 scopus 로고
    • Partial enzymatic hydrolysis of whey protein by trypsin
    • Jost R, Monti JC and Pahud JJ, Partial enzymatic hydrolysis of whey protein by trypsin. J Dairy Sci 60:1387-1393 (1977).
    • (1977) J Dairy Sci , vol.60 , pp. 1387-1393
    • Jost, R.1    Monti, J.C.2    Pahud, J.J.3
  • 46
    • 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 and 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 102:1317-1327 (2007).
    • (2007) Food Chem , vol.102 , pp. 1317-1327
    • Klompong, V.1    Benjakul, S.2    Kantachote, D.3    Shahidi, F.4
  • 47
    • 34249088376 scopus 로고    scopus 로고
    • Influence of the extent of enzymatic hydrolysis on the functional properties of protein hydrolysate from grass carp (Ctenopharyngodon idella) skin
    • Wasswa J, Tang J, Gu XH and Yuan XQ, Influence of the extent of enzymatic hydrolysis on the functional properties of protein hydrolysate from grass carp (Ctenopharyngodon idella) skin. Food Chem 104:1698-1704 (2007).
    • (2007) Food Chem , vol.104 , pp. 1698-1704
    • Wasswa, J.1    Tang, J.2    Gu, X.H.3    Yuan, X.Q.4
  • 48
    • 84963187703 scopus 로고
    • Functional properties of proteins in food: A survey
    • Kinsella JE, Functional properties of proteins in food: a survey. Crit Rev Food Sci Nutr 8:219-280 (1976).
    • (1976) Crit Rev Food Sci Nutr , vol.8 , pp. 219-280
    • Kinsella, J.E.1
  • 49
    • 23744506273 scopus 로고    scopus 로고
    • Functional and nutritional properties of red salmon (Oncorhynchus nerka) enzymatic hydrolysates
    • Sathivel S, Smiley S, PrinyawiwatkulW and Bechtel PJ, Functional and nutritional properties of red salmon (Oncorhynchus nerka) enzymatic hydrolysates. J Food Sci 6:401-406 (2005).
    • (2005) J Food Sci , vol.6 , pp. 401-406
    • Sathivel, S.1    Smiley, S.2    Prinyawiwatkul, W.3    Bechtel, P.J.4
  • 50
    • 0027349531 scopus 로고
    • Influence of milk peptides in determining the functionality of milk proteins: A review
    • Haque ZU, Influence of milk peptides in determining the functionality of milk proteins: a review. J Dairy Sci 76:311-320 (1993).
    • (1993) J Dairy Sci , vol.76 , pp. 311-320
    • Haque, Z.U.1
  • 52
    • 85025553351 scopus 로고
    • Casein hydrolysate. II. Functional properties of peptides
    • Haque ZUand Mozaffar Z, Casein hydrolysate. II. Functional properties of peptides. Food Hydrocolloids 5:559-571 (1992).
    • (1992) Food Hydrocolloids , vol.5 , pp. 559-571
    • Haque, Z.U.1    Mozaffar, Z.2
  • 53
    • 0033630245 scopus 로고    scopus 로고
    • Fish protein hydrolysates: Production, biochemical, and functional properties
    • Kristinsson HG and Rasco BA, Fish protein hydrolysates: production, biochemical, and functional properties. Crit Rev Food Sci Nutr 1:43-81 (2000).
    • (2000) Crit Rev Food Sci Nutr , vol.1 , pp. 43-81
    • Kristinsson, H.G.1    Rasco, B.A.2
  • 56
    • 0016608047 scopus 로고
    • Angiotensin-I converting enzyme
    • Erdös EG, Angiotensin-I converting enzyme. Circ Res 36:247-255 (1975).
    • (1975) Circ Res , vol.36 , pp. 247-255
    • Erdös, E.G.1
  • 57
    • 0014959663 scopus 로고
    • Isolation of bradykinin potentiating peptides from Bothrops jararaca venom
    • Ferreira SH, Bartelt DC and Greene LJ, Isolation of bradykinin potentiating peptides from Bothrops jararaca venom. Biochemistry 9:2583-2593 (1970).
    • (1970) Biochemistry , vol.9 , pp. 2583-2593
    • Ferreira, S.H.1    Bartelt, D.C.2    Greene, L.J.3
  • 58
    • 0033823597 scopus 로고    scopus 로고
    • Production of angiotensin converting enzyme inhibitory peptides in fermented milks started by Lactobacillus delbrueckii subsp. bulgaricus SS1 and Lactococcus lactis subsp. cremoris FT4
    • Gobbetti M, Ferranti P, Smacchi E, Goffredi F and Addeo F, Production of angiotensin converting enzyme inhibitory peptides in fermented milks started by Lactobacillus delbrueckii subsp. bulgaricus SS1 and Lactococcus lactis subsp. cremoris FT4. Appl Environ Microbiol 66:3898-3904 (2000).
    • (2000) Appl Environ Microbiol , vol.66 , pp. 3898-3904
    • Gobbetti, M.1    Ferranti, P.2    Smacchi, E.3    Goffredi, F.4    Addeo, F.5
  • 59
    • 8844258885 scopus 로고    scopus 로고
    • Caseins as source of bioactive peptides
    • Silva SV and Malcata FX, Caseins as source of bioactive peptides. Int Dairy J 15:1-15 (2005).
    • (2005) Int Dairy J , vol.15 , pp. 1-15
    • Silva, S.V.1    Malcata, F.X.2
  • 61
    • 2342569607 scopus 로고    scopus 로고
    • A quantitative in silico analysis calculates the angiotensin I converting enzyme (ACE) inhibitory activity in pea and whey protein digests
    • Vermeirssen VA, van der Bent A, Van Camp J, van Amerongen A and Verstraete W, A quantitative in silico analysis calculates the angiotensin I converting enzyme (ACE) inhibitory activity in pea and whey protein digests. Biochimie 86:231-239 (2004).
    • (2004) Biochimie , vol.86 , pp. 231-239
    • Vermeirssen, V.A.1    van der Bent, A.2    van Camp, J.3    van Amerongen, A.4    Verstraete, W.5
  • 62
    • 0035545394 scopus 로고    scopus 로고
    • Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins
    • Arihara K, Nakashima Y, Mukai T, Ishikawa S and Itoh M, Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins. Meat Sci 57:319-324 (2001).
    • (2001) Meat Sci , vol.57 , pp. 319-324
    • Arihara, K.1    Nakashima, Y.2    Mukai, T.3    Ishikawa, S.4    Itoh, M.5
  • 63
    • 0346752503 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce
    • Ichimura T, Hu JE, Aita DQ and Maruyama S, Angiotensin I-converting enzyme inhibitory activity and insulin secretion stimulative activity of fermented fish sauce. J Biosci Bioeng 96:496-499 (2003).
    • (2003) J Biosci Bioeng , vol.96 , pp. 496-499
    • Ichimura, T.1    Hu, J.E.2    Aita, D.Q.3    Maruyama, S.4
  • 64
    • 2542580915 scopus 로고    scopus 로고
    • Production of angiotensin I converting enzyme inhibitory peptides from sea bream scales
    • Kuba M, Tana C, Tawata S and Yasuda M, Production of angiotensin I converting enzyme inhibitory peptides from sea bream scales. Process Biochem 39:1195-1200 (2004).
    • (2004) Process Biochem , vol.39 , pp. 1195-1200
    • Kuba, M.1    Tana, C.2    Tawata, S.3    Yasuda, M.4
  • 65
    • 13844322374 scopus 로고    scopus 로고
    • Production of angiotensin I-converting enzyme inhibitory peptides from soybean protein with Monascus purpureus acid proteinase
    • Kuba M, Tana C, Tawata S and Yasuda M, Production of angiotensin I-converting enzyme inhibitory peptides from soybean protein with Monascus purpureus acid proteinase. Process Biochem 40:2191-2196 (2005).
    • (2005) Process Biochem , vol.40 , pp. 2191-2196
    • Kuba, M.1    Tana, C.2    Tawata, S.3    Yasuda, M.4
  • 66
    • 34548243982 scopus 로고    scopus 로고
    • High throughput and rapid screening of marine protein hydrolysates enriched in peptides with angiotensin-I-converting enzyme inhibitory activity by capillary electrophoresis
    • He HL, Chen XL, Wu H, Sun CY, Zhang YZ and Zhou BC, High throughput and rapid screening of marine protein hydrolysates enriched in peptides with angiotensin-I-converting enzyme inhibitory activity by capillary electrophoresis. Bioresour Technol 98:3499-3505 (2007).
    • (2007) Bioresour Technol , vol.98 , pp. 3499-3505
    • He, H.L.1    Chen, X.L.2    Wu, H.3    Sun, C.Y.4    Zhang, Y.Z.5    Zhou, B.C.6
  • 67
    • 0026936217 scopus 로고
    • Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito
    • Yokoyama K, Chiba H, Yoshikawa K, Chiba H and Yoshikawa M, Peptide inhibitors for angiotensin I-converting enzyme from thermolysin digest of dried bonito. Biosci Biotechnol Biochem 56:1541-1545 (1992).
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 1541-1545
    • Yokoyama, K.1    Chiba, H.2    Yoshikawa, K.3    Chiba, H.4    Yoshikawa, M.5
  • 68
    • 33644905566 scopus 로고    scopus 로고
    • Inhibition properties of dipeptides from salmon muscle hydrolysate on angiotensin I-converting enzyme
    • Ono S, Hosokawa M, Miyashita K and Takahashi K, Inhibition properties of dipeptides from salmon muscle hydrolysate on angiotensin I-converting enzyme. Int J Food Sci Technol 41:383-386 (2006).
    • (2006) Int J Food Sci Technol , vol.41 , pp. 383-386
    • Ono, S.1    Hosokawa, M.2    Miyashita, K.3    Takahashi, K.4
  • 69
    • 0028712310 scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardinemuscle
    • Matsufuji H, Matsui T, Seki E, Osajima K, Nakashima M and Osajima Y, Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardinemuscle. Biosci Biotechnol Biochem 58:2244-2245 (1994).
    • (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
  • 70
    • 0030127886 scopus 로고    scopus 로고
    • Enhancing thefunctionalityof foodproteins by enzymaticmodification
    • Panyam DandKilara A, Enhancing thefunctionalityof foodproteins by enzymaticmodification. Trends Food Sci Technol 7:120-125 (1996).
    • (1996) Trends Food Sci Technol , vol.7 , pp. 120-125
    • Panyam, D.1    Kilara, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.