메뉴 건너뛰기




Volumn 51, Issue 2, 2014, Pages 276-284

Optimization of some conditions of Neutrase-catalyzed plastein reaction to mediate ACE-inhibitory activity in vitro of casein hydrolysate prepared by Neutrase

Author keywords

ACE inhibitory activity; Casein; Casein hydrolysate; Neutrase; Plastein reaction

Indexed keywords

CASEIN; CATALYSIS; HYDROLYSIS; PEPTIDES;

EID: 84897655686     PISSN: 00221155     EISSN: 09758402     Source Type: Journal    
DOI: 10.1007/s13197-011-0503-0     Document Type: Article
Times cited : (28)

References (46)
  • 1
    • 0018536145 scopus 로고
    • Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid
    • 1:CAS:528:DyaE1MXlvFWnsbw%3D 10.1021/jf60226a042
    • Adler-Nissen J (1979) Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J Agric Food Chem 27:1256-1261
    • (1979) J Agric Food Chem , vol.27 , pp. 1256-1261
    • Adler-Nissen, J.1
  • 2
    • 0025056650 scopus 로고
    • The plastein reaction revisited: Evidence for a purely aggregation reaction mechanism
    • 1:CAS:528:DyaK3cXhtFOnu74%3D 10.1016/0308-8146(90)90015-V
    • Andrews AT, Alichanidis E (1990) The plastein reaction revisited: evidence for a purely aggregation reaction mechanism. Food Chem 35:243-261
    • (1990) Food Chem , vol.35 , pp. 243-261
    • Andrews, A.T.1    Alichanidis, E.2
  • 3
    • 0027596904 scopus 로고
    • Angiotensin-converting enzyme inhibitors derived from food proteins
    • 1:CAS:528:DyaK3sXlsFynsLs%3D 10.1016/0924-2244(93)90033-7
    • Ariyoshi Y (1993) Angiotensin-converting enzyme inhibitors derived from food proteins. Trends Food Sci Tech 4:139-144
    • (1993) Trends Food Sci Tech , vol.4 , pp. 139-144
    • Ariyoshi, Y.1
  • 4
    • 0020534342 scopus 로고
    • Amino acid-enriched plasteins: A source of limiting amino acids for the weanling rat
    • 1:CAS:528:DyaL3sXovVSntA%3D%3D
    • Ashley DVM, Temler R, Barclay D, Dormond CA, Jost R (1983) Amino acid-enriched plasteins: a source of limiting amino acids for the weanling rat. J Nutr 113:21-27
    • (1983) J Nutr , vol.113 , pp. 21-27
    • Ashley, D.V.M.1    Temler, R.2    Barclay, D.3    Dormond, C.A.4    Jost, R.5
  • 5
    • 0019332139 scopus 로고
    • Binding of peptide substrates and inhibitors of angiotensin converting enzyme
    • 1:CAS:528:DyaL3cXht1eqtbY%3D
    • Cheung HS, Wang FL, Ondetti MA, Sabo E, Cushman DW (1980) Binding of peptide substrates and inhibitors of angiotensin converting enzyme. J Biol Chem 255:401-407
    • (1980) J Biol Chem , vol.255 , pp. 401-407
    • Cheung, H.S.1    Wang, F.L.2    Ondetti, M.A.3    Sabo, E.4    Cushman, D.W.5
  • 6
    • 85022241054 scopus 로고
    • Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins
    • 1:CAS:528:DyaL3sXksFWqt7k%3D 10.3168/jds.S0022-0302(83)81926-2
    • Church FC, Swaisgood HE, Porter DH, Catignani GL (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
  • 7
    • 0027081860 scopus 로고
    • α-Chymotrypsin in plastein synthesis. Influence of water activity
    • 1:CAS:528:DyaK3sXkslSnsbY%3D 10.1111/j.1749-6632.1992.tb32706.x (Enzyme Engineering XI)
    • Combes D, Lozano P (1992) α-Chymotrypsin in plastein synthesis. Influence of water activity. Ann NY Acad Sci 672:409-414 (Enzyme Engineering XI)
    • (1992) Ann NY Acad Sci , vol.672 , pp. 409-414
    • Combes, D.1    Lozano, P.2
  • 8
    • 67650214679 scopus 로고    scopus 로고
    • Novel casein-derived peptides with antihypertensive activity
    • 1:CAS:528:DC%2BD1MXoslaktrc%3D 10.1016/j.idairyj.2009.05.004
    • Contreras MM, Carrón R, Montero MJ, Ramos M, Recio I (2009) Novel casein-derived peptides with antihypertensive activity. Int Dairy J 19:566-573
    • (2009) Int Dairy J , vol.19 , pp. 566-573
    • Contreras, M.M.1    Carrón, R.2    Montero, M.J.3    Ramos, M.4    Recio, I.5
  • 9
    • 33847159988 scopus 로고    scopus 로고
    • Effect of heat and enzymatic treatment on the antihypertensive activity of whey protein hydrolysates
    • 10.1016/j.idairyj.2006.09.003
    • da Costa EL, Gontijo JAD, Netto FM (2007) Effect of heat and enzymatic treatment on the antihypertensive activity of whey protein hydrolysates. Int Dairy J 17:632-640
    • (2007) Int Dairy J , vol.17 , pp. 632-640
    • Da Costa, E.L.1    Gontijo, J.A.D.2    Netto, F.M.3
  • 10
    • 84891273387 scopus 로고    scopus 로고
    • Optimization of the production of shrimp waste protein hydrolysate using microbial proteases adopting response surface methodology
    • DOI: 10.1007/s13197-011-0455-4
    • Dey SS, Dora KC (2011) Optimization of the production of shrimp waste protein hydrolysate using microbial proteases adopting response surface methodology. J Food Sci Technol, available online (DOI: 10.1007/s13197-011-0455- 4)
    • (2011) J Food Sci Technol
    • Dey, S.S.1    Dora, K.C.2
  • 11
    • 1842478225 scopus 로고    scopus 로고
    • Hypotensive peptides from milk proteins
    • 1:CAS:528:DC%2BD2cXjtFOrs7c%3D
    • FitzGerald RJ, Murray BA, Walsh DJ (2004) Hypotensive peptides from milk proteins. J Nutr 134:980S-988S
    • (2004) J Nutr , vol.134
    • Fitzgerald, R.J.1    Murray, B.A.2    Walsh, D.J.3
  • 12
    • 0015032152 scopus 로고
    • Application of microbial proteinase to soybean and other materials to improve acceptability
    • 1:CAS:528:DyaE3MXkslGjtbg%3D 10.1111/j.1365-2672.1971.tb02272.x
    • Fujimaki M, Kato M, Aria S, Yamashita M (1971) Application of microbial proteinase to soybean and other materials to improve acceptability. J Appl Bacteriol 34:119-131
    • (1971) J Appl Bacteriol , vol.34 , pp. 119-131
    • Fujimaki, M.1    Kato, M.2    Aria, S.3    Yamashita, M.4
  • 13
    • 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
    • 1:CAS:528:DC%2BD1MXmvVChtQ%3D%3D 10.1016/j.foodchem.2008.09.041
    • Guo Y, Pan D, Tanokura M (2009) 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 114:328-333
    • (2009) Food Chem , vol.114 , pp. 328-333
    • Guo, Y.1    Pan, D.2    Tanokura, M.3
  • 14
    • 84883142117 scopus 로고
    • Determination of the nitrogen (Kjeldahl method) and calculation of the crude protein content
    • IDF Brussels, Belgium
    • IDF (1993) Determination of the nitrogen (Kjeldahl method) and calculation of the crude protein content. In: IDF Standard 20B. International Dairy Federation, Brussels, Belgium
    • (1993) IDF Standard 20B. International Dairy Federation
  • 16
    • 33846953603 scopus 로고    scopus 로고
    • Yak milk casein as a functional ingredient: Preparation and identification of angiotensin-I-converting enzyme inhibitory peptides
    • 1:CAS:528:DC%2BD2sXhsFCqsbk%3D 10.1017/S0022029906002056
    • Jiang J, Chen S, Ren F, Luo Z, Zeng SS (2007) Yak milk casein as a functional ingredient: preparation and identification of angiotensin-I- converting enzyme inhibitory peptides. J Dairy Res 74:18-25
    • (2007) J Dairy Res , vol.74 , pp. 18-25
    • Jiang, J.1    Chen, S.2    Ren, F.3    Luo, Z.4    Zeng, S.S.5
  • 17
    • 3242745355 scopus 로고    scopus 로고
    • Protein modification to optimize functionality: Protein hydrolysates
    • J.R. Whitaker A.F.J. Voragen D.W.S. Wong (eds) Marcel Dekker Now York
    • Kunst T (2003) Protein modification to optimize functionality: protein hydrolysates. In: Whitaker JR, Voragen AFJ, Wong DWS (eds) Handbook of food enzymology. Marcel Dekker, Now York, pp 221-236
    • (2003) Handbook of Food Enzymology , pp. 221-236
    • Kunst, T.1
  • 18
    • 33748297647 scopus 로고    scopus 로고
    • Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity
    • 10.1016/j.idairyj.2006.06.004
    • López-Fandiño R, Otte J, van Camp J (2006) Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity. Int Dairy J 16:1277-1293
    • (2006) Int Dairy J , vol.16 , pp. 1277-1293
    • López-Fandiño, R.1    Otte, J.2    Van Camp, J.3
  • 19
    • 0026236910 scopus 로고
    • α-Chymotrypsin in plastein synthesis: Influence of substrate concentration on enzyme activity
    • 1:CAS:528:DyaK3MXmslCgt7Y%3D
    • Lozano P, Combes D (1991) α-Chymotrypsin in plastein synthesis: influence of substrate concentration on enzyme activity. Biotechnol Appl Biochem 14:212-221
    • (1991) Biotechnol Appl Biochem , vol.14 , pp. 212-221
    • Lozano, P.1    Combes, D.2
  • 20
    • 33947517284 scopus 로고    scopus 로고
    • Value-added utilization of yak milk casein for the production of angiotensin-I-converting enzyme inhibitory peptides
    • 1:CAS:528:DC%2BD2sXjs1Cqtrw%3D 10.1016/j.foodchem.2006.10.041
    • Mao XY, Ni JR, Sun WL, Hao PP, Fan L (2007) Value-added utilization of yak milk casein for the production of angiotensin-I-converting enzyme inhibitory peptides. Food Chem 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
  • 21
    • 57249089073 scopus 로고    scopus 로고
    • An in-vitro investigation of selected biological activities of hydrolysed flaxseed (Linum usitatissimum L.) proteins
    • 1:CAS:528:DC%2BD1cXhsVenurrF 10.1007/s11746-008-1293-z
    • Marambe PWMLHK, Shand PJ, Wanasundara JPD (2008) An in-vitro investigation of selected biological activities of hydrolysed flaxseed (Linum usitatissimum L.) proteins. J Am Oil Chem Soc 85:1155-1164
    • (2008) J Am Oil Chem Soc , vol.85 , pp. 1155-1164
    • Marambe, P.1    Shand, P.J.2    Wanasundara, J.P.D.3
  • 22
    • 0001586967 scopus 로고    scopus 로고
    • Biochemical properties of bioactive peptides derived from milk proteins: Potential nutraceuticals for food and pharmaceutical applications
    • 10.1016/S0301-6226(97)00083-3
    • Meisel H (1997) Biochemical properties of bioactive peptides derived from milk proteins: potential nutraceuticals for food and pharmaceutical applications. Livest Prod Sci 50:125-138
    • (1997) Livest Prod Sci , vol.50 , pp. 125-138
    • Meisel, H.1
  • 23
    • 47749104885 scopus 로고    scopus 로고
    • ACE - Inhibitory and antihypertensive properties of a bovine casein hydrolysate
    • 1:CAS:528:DC%2BD1cXovFyjtLo%3D 10.1016/j.foodchem.2008.05.041
    • Miguel M, Contreras MM, Recio I, Aleixandre A (2009) ACE - inhibitory and antihypertensive properties of a bovine casein hydrolysate. Food Chem 112:211-214
    • (2009) Food Chem , vol.112 , pp. 211-214
    • Miguel, M.1    Contreras, M.M.2    Recio, I.3    Aleixandre, A.4
  • 24
    • 1842626386 scopus 로고    scopus 로고
    • Modification of the furanacryloyl-L- phenylalanyl-glycylglycine assay for determination of angiotensin-I-converting enzyme inhibitory activity
    • 1:CAS:528:DC%2BD2cXktF2ls7c%3D 10.1016/j.jbbm.2003.12.009
    • Murray BA, Walsh DJ, FitzGerald RJ (2004) Modification of the furanacryloyl-L- phenylalanyl-glycylglycine assay for determination of angiotensin-I-converting enzyme inhibitory activity. J Biochem Biophys Meth 59:127-137
    • (2004) J Biochem Biophys Meth , vol.59 , pp. 127-137
    • Murray, B.A.1    Walsh, D.J.2    Fitzgerald, R.J.3
  • 25
    • 0029286291 scopus 로고
    • Purification and characterization of angiotensin-I converting enzyme inhibitors from a sour milk
    • 1:CAS:528:DyaK2MXlt1Cks7g%3D 10.3168/jds.S0022-0302(95)76689-9
    • Nakamura Y, Yamamoto N, Sakai K, Okubo A, Yamazaki S, Takano T (1995) Purification and characterization of angiotensin-I converting enzyme inhibitors from a sour milk. J Dairy Sci 78:777-783
    • (1995) J Dairy Sci , vol.78 , pp. 777-783
    • Nakamura, Y.1    Yamamoto, N.2    Sakai, K.3    Okubo, A.4    Yamazaki, S.5    Takano, T.6
  • 26
    • 84881067529 scopus 로고    scopus 로고
    • Antioxidant and functional properties of protein hydrolysates from pink perch (Nemipterus japonicus) muscle
    • DOI: 10.1007/s13197-011-0416-y
    • Naqash SY, Nazeer RA (2011) Antioxidant and functional properties of protein hydrolysates from pink perch (Nemipterus japonicus) muscle. J Food Sci Technol, available online (DOI: 10.1007/s13197-011-0416-y)
    • (2011) J Food Sci Technol
    • Naqash, S.Y.1    Nazeer, R.A.2
  • 28
    • 33846024711 scopus 로고    scopus 로고
    • Angiotensin- converting enzyme inhibitory activity of milk protein hydrolysates: Effect of substrate, enzyme and time of hydrolysis
    • 1:CAS:528:DC%2BD2sXis1aqsw%3D%3D 10.1016/j.idairyj.2006.05.011
    • Otte J, Shalaby SM, Zakora M, Pripp AH, El-Shabrawy SA (2007) Angiotensin- converting enzyme inhibitory activity of milk protein hydrolysates: effect of substrate, enzyme and time of hydrolysis. Int Dairy J 17:488-503
    • (2007) Int Dairy J , vol.17 , pp. 488-503
    • Otte, J.1    Shalaby, S.M.2    Zakora, M.3    Pripp, A.H.4    El-Shabrawy, S.A.5
  • 29
    • 84985407594 scopus 로고
    • Plastein synthesis with α-chymotrypsin immobilised on chitin
    • 1:CAS:528:DyaL3cXkvFelsLw%3D 10.1002/jsfa.2740310311
    • Pallavicini C, Finley JW, Stanley WL, Watters GG (1980) Plastein synthesis with α-chymotrypsin immobilised on chitin. J Sci Food Agric 31:273-278
    • (1980) J Sci Food Agric , vol.31 , pp. 273-278
    • Pallavicini, C.1    Finley, J.W.2    Stanley, W.L.3    Watters, G.G.4
  • 30
    • 70450257667 scopus 로고    scopus 로고
    • Angiotensin i converting enzyme (ACE) inhibitory activity and antihypertensive effect of fermented milk
    • 1:CAS:528:DC%2BD1MXhsVymt7%2FJ 10.1016/j.idairyj.2009.07.003
    • Pihlanto A, Virtanen T, Korhonen H (2010) Angiotensin I converting enzyme (ACE) inhibitory activity and antihypertensive effect of fermented milk. Int Dairy J 20:3-10
    • (2010) Int Dairy J , vol.20 , pp. 3-10
    • Pihlanto, A.1    Virtanen, T.2    Korhonen, H.3
  • 31
    • 84878481500 scopus 로고    scopus 로고
    • Optimization of gelatin extraction from chicken deboner residue using RSM method
    • DOI: 10.1007/s13197-011-0355-7
    • Rafieian F, Keramat J, Kadivar M (2011) Optimization of gelatin extraction from chicken deboner residue using RSM method. J Food Sci Technol, available online (DOI: 10.1007/s13197-011-0355-7)
    • (2011) J Food Sci Technol
    • Rafieian, F.1    Keramat, J.2    Kadivar, M.3
  • 32
    • 8444246337 scopus 로고    scopus 로고
    • Identification of angiotensin- I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765
    • 1:CAS:528:DC%2BD2cXosVOktL8%3D 10.1021/jf049510t
    • Robert MC, Razaname A, Mutter M, Juillerat MA (2004) Identification of angiotensin- I-converting enzyme inhibitory peptides derived from sodium caseinate hydrolysates produced by Lactobacillus helveticus NCC 2765. J Agric Food Chem 52:6923-6931
    • (2004) J Agric Food Chem , vol.52 , pp. 6923-6931
    • Robert, M.C.1    Razaname, A.2    Mutter, M.3    Juillerat, M.A.4
  • 34
    • 33646464385 scopus 로고    scopus 로고
    • Performance of two commonly used angiotensin- converting enzyme inhibition assays using FA-PGG and HHL as substrates
    • 1:CAS:528:DC%2BD28Xkt1Kjtrg%3D 10.1017/S0022029905001639
    • Shalaby SM, Zakora M, Otte J (2006) Performance of two commonly used angiotensin- converting enzyme inhibition assays using FA-PGG and HHL as substrates. J Dairy Res 73:178-186
    • (2006) J Dairy Res , vol.73 , pp. 178-186
    • Shalaby, S.M.1    Zakora, M.2    Otte, J.3
  • 35
    • 0038029531 scopus 로고    scopus 로고
    • Proteinase and exopeptidase hydrolysis of whey protein: Comparison of the TNBS, OPA and pH stat methods for quantification of degree of hydrolysis
    • 1:CAS:528:DC%2BD3sXjsVGmtb4%3D 10.1016/S0958-6946(03)00053-0
    • Spellman D, McEvoy E, O'Cuinn G, FitzGerald RJ (2003) Proteinase and exopeptidase hydrolysis of whey protein: comparison of the TNBS, OPA and pH stat methods for quantification of degree of hydrolysis. Int Dairy J 13:447-453
    • (2003) Int Dairy J , vol.13 , pp. 447-453
    • Spellman, D.1    McEvoy, E.2    O'Cuinn, G.3    Fitzgerald, R.J.4
  • 36
    • 0033180421 scopus 로고    scopus 로고
    • Use of NMR and mass spectrometry to detect and quantify protease-catalyzed peptide bond formation in complex mixtures
    • 1:CAS:528:DyaK1MXlsVOmurc%3D 10.1016/S0141-0229(99)00053-8
    • Stevenson DE, Morgan KR, Fenton GA, Moraes G (1999) Use of NMR and mass spectrometry to detect and quantify protease-catalyzed peptide bond formation in complex mixtures. Enzyme Microb Technol 25:357-363
    • (1999) Enzyme Microb Technol , vol.25 , pp. 357-363
    • Stevenson, D.E.1    Morgan, K.R.2    Fenton, G.A.3    Moraes, G.4
  • 37
    • 0033695674 scopus 로고    scopus 로고
    • Identification of an antihypertensive peptide from peptic digest of wakame (Undaria pinnatifida)
    • 1:CAS:528:DC%2BD3cXot1yhsrs%3D 10.1016/S0955-2863(00)00110-8
    • Suetsuna K, Nakano T (2000) Identification of an antihypertensive peptide from peptic digest of wakame (Undaria pinnatifida). J Nutr Biochem 11:450-454
    • (2000) J Nutr Biochem , vol.11 , pp. 450-454
    • Suetsuna, K.1    Nakano, T.2
  • 38
    • 84974224136 scopus 로고
    • Application of the plastein reaction to caseins and to skim milk powder I. Protein hydrolysis and plastein formation
    • 1:CAS:528:DyaL38Xkt1ags78%3D 10.1017/S0022029900022366
    • Sukan G, Andrews AT (1982a) Application of the plastein reaction to caseins and to skim milk powder I. Protein hydrolysis and plastein formation. J Dairy Res 49:265-278
    • (1982) J Dairy Res , vol.49 , pp. 265-278
    • Sukan, G.1    Andrews, A.T.2
  • 39
    • 84974325042 scopus 로고
    • Application of the plastein reaction to caseins and to skim milk powder II. Chemical and physical properties of the plasteins
    • 1:CAS:528:DyaL38Xkt1ags7w%3D 10.1017/S0022029900022378
    • Sukan G, Andrews AT (1982b) Application of the plastein reaction to caseins and to skim milk powder II. Chemical and physical properties of the plasteins. J Dairy Res 49:279-293
    • (1982) J Dairy Res , vol.49 , pp. 279-293
    • Sukan, G.1    Andrews, A.T.2
  • 40
    • 79958258921 scopus 로고    scopus 로고
    • Antioxidant activity of hydrolysates and peptide fractions derived from porcine hemoglobin
    • 1:CAS:528:DC%2BC3cXhs1WnurnO 10.1007/s13197-010-0115-0
    • Sun Q, Shen H, Luo Y (2011) Antioxidant activity of hydrolysates and peptide fractions derived from porcine hemoglobin. J Food Sci Tech 48:53-60
    • (2011) J Food Sci Tech , vol.48 , pp. 53-60
    • Sun, Q.1    Shen, H.2    Luo, Y.3
  • 41
    • 0035132362 scopus 로고    scopus 로고
    • Application of the plastein reaction to mycoprotein: I. Plastein synthesis
    • 1:CAS:528:DC%2BD3MXmvFKntw%3D%3D 10.1016/S0308-8146(00)00233-8
    • Williams RJH, Brownsell VL, Andrews AT (2001) Application of the plastein reaction to mycoprotein: I. Plastein synthesis. Food Chem 72:329-335
    • (2001) Food Chem , vol.72 , pp. 329-335
    • Williams, R.J.H.1    Brownsell, V.L.2    Andrews, A.T.3
  • 42
    • 0030873439 scopus 로고    scopus 로고
    • Antihypertensive peptides derived from food proteins
    • 1:CAS:528:DyaK2sXktFCktL8%3D 10.1002/(SICI)1097-0282(1997)43:2<129: AID-BIP5>3.0.CO;2-X
    • Yamamoto N (1997) Antihypertensive peptides derived from food proteins. Biopolymers 43:129-134
    • (1997) Biopolymers , vol.43 , pp. 129-134
    • Yamamoto, N.1
  • 43
    • 33847799978 scopus 로고
    • Plastein reaction for food protein improvement
    • 1:CAS:528:DyaE28XlslGrsrc%3D 10.1021/jf60208a038
    • Yamashita M, Arai S, Fujimaki M (1976a) Plastein reaction for food protein improvement. J Agric Food Chem 24:1100-1104
    • (1976) J Agric Food Chem , vol.24 , pp. 1100-1104
    • Yamashita, M.1    Arai, S.2    Fujimaki, M.3
  • 44
    • 84985164251 scopus 로고
    • A low-phenylalenine, high-tyrosine plastein as an acceptable dietetic food
    • 1:CAS:528:DyaE28XlsFyitLs%3D 10.1111/j.1365-2621.1976.tb14382.x
    • Yamashita M, Arai S, Fujimaki M (1976b) A low-phenylalenine, high-tyrosine plastein as an acceptable dietetic food. J Food Sci 41:1029-1032
    • (1976) J Food Sci , vol.41 , pp. 1029-1032
    • Yamashita, M.1    Arai, S.2    Fujimaki, M.3
  • 45
    • 0015148275 scopus 로고
    • Plastein reaction as a method for enhancing the sulfur-containing amino acid level of soybean protein
    • 10.1021/jf60178a029
    • Ymashita M, Arai S, Tsai SJ, Fujimaki M (1971) Plastein reaction as a method for enhancing the sulfur-containing amino acid level of soybean protein. J Agric Food Chem 19:1151-1154
    • (1971) J Agric Food Chem , vol.19 , pp. 1151-1154
    • Ymashita, M.1    Arai, S.2    Tsai, S.J.3    Fujimaki, M.4
  • 46
    • 70349986477 scopus 로고    scopus 로고
    • An approach to improve ACE-inhibitory activity of casein hydrolysates with plastein reaction catalyzed by Alcalase
    • 1:CAS:528:DC%2BD1MXhtVSitbfM 10.1007/s00217-009-1110-4
    • Zhao XH, Li YY (2009) An approach to improve ACE-inhibitory activity of casein hydrolysates with plastein reaction catalyzed by Alcalase. Euro Food Res Tech 229:795-805
    • (2009) Euro Food Res Tech , vol.229 , pp. 795-805
    • Zhao, X.H.1    Li, Y.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.