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Volumn 5, Issue 1, 2015, Pages 63-69

Mechanisms of plastein formation, and prospective food and nutraceutical applications of the peptide aggregates

Author keywords

Bioactivity; Debittering; Nutraceutical; Nutritional enrichment; Peptide aggregation; Plastein

Indexed keywords

CASEIN HYDROLYSATE; CHITIN; CHYMOTRYPSIN A; NUTRACEUTICAL; PEPTIDE; PLASTEIN; PROTEIN; PROTEINASE; SOYBEAN PROTEIN; UNCLASSIFIED DRUG;

EID: 84926395584     PISSN: None     EISSN: 2215017X     Source Type: Journal    
DOI: 10.1016/j.btre.2014.12.003     Document Type: Review
Times cited : (42)

References (62)
  • 1
    • 0025056650 scopus 로고
    • The plastein reaction revisited: Evidence for a purely aggregation reaction mechanism
    • A. T. Andrews, E. Alichanidis, The plastein reaction revisited: evidence for a purely aggregation reaction mechanism, Food Chem. 35 (4) (1990) 243-261.
    • (1990) Food Chem. , vol.35 , Issue.4 , pp. 243-261
    • Andrews, A.T.1    Alichanidis, E.2
  • 2
    • 0020534342 scopus 로고
    • Amino acidenriched plasteins: A source of limiting amino acids for the weanling rat
    • D. V. M. Ashley, R. Temler, D. Barclay, C. A. Dormond, R. Jost, Amino acidenriched plasteins: a source of limiting amino acids for the weanling rat, J. Nutr. 113 (1) (1983) 21-27.
    • (1983) J. Nutr. , vol.113 , Issue.1 , pp. 21-27
    • Ashley, D.V.M.1    Temler, R.2    Barclay, D.3    Dormond, C.A.4    Jost, R.5
  • 3
    • 0016242670 scopus 로고
    • Hydrophobic force as a main factor contributing to plastein chain assembly
    • K. Aso, M. Yamashita, S. Arai, M. Fujimaki, Hydrophobic force as a main factor contributing to plastein chain assembly, J. Biochem. 76 (2) (1974) 341-347.
    • (1974) J. Biochem. , vol.76 , Issue.2 , pp. 341-347
    • Aso, K.1    Yamashita, M.2    Arai, S.3    Fujimaki, M.4
  • 4
    • 0016168002 scopus 로고
    • Tryptophan-, threonine-, and lysineenriched plasteins from zein
    • K. Aso, M. Yamashita, S. Arai, M. Fujimaki, Tryptophan-, threonine-, and lysineenriched plasteins from zein, Agric. Biol. Chem. 38 (3) (1974) 679-680.
    • (1974) Agric. Biol. Chem. , vol.38 , Issue.3 , pp. 679-680
    • Aso, K.1    Yamashita, M.2    Arai, S.3    Fujimaki, M.4
  • 5
    • 84892140755 scopus 로고
    • The nutritive value of plastein
    • H. H. Beard, The nutritive value of plastein, J. Biol. Chem. 71 (2) (1927) 477-480.
    • (1927) J. Biol. Chem. , vol.71 , Issue.2 , pp. 477-480
    • Beard, H.H.1
  • 6
    • 0035136955 scopus 로고    scopus 로고
    • Application of the plastein reaction to mycoprotein: II. Plastein properties
    • V. L. Brownsell, R. J. H. Williams, A. T. Andrews, Application of the plastein reaction to mycoprotein: II. Plastein properties, Food Chem. 72 (3) (2001) 337-346.
    • (2001) Food Chem. , vol.72 , Issue.3 , pp. 337-346
    • Brownsell, V.L.1    Williams, R.J.H.2    Andrews, A.T.3
  • 8
    • 0027081860 scopus 로고
    • α-Chymotrypsin in plastein synthesis influence ofwater activity
    • D. Combes, P. Lozano, α-Chymotrypsin in plastein synthesis influence ofwater activity, Ann. N. Y. Acad. Sci. 672 (1) (1992) 409-414.
    • (1992) Ann. N. Y. Acad. Sci. , vol.672 , Issue.1 , pp. 409-414
    • Combes, D.1    Lozano, P.2
  • 9
    • 0141674942 scopus 로고    scopus 로고
    • Enzyme-induced gelation of extensively hydrolyzed whey proteins by alcalase: Comparison with the plastein reaction and characterization of interactions
    • D. Doucet, S. F. Gauthier, D. Otter, E. A. Foegeding, Enzyme-induced gelation of extensively hydrolyzed whey proteins by alcalase: comparison with the plastein reaction and characterization of interactions, J. Agric. Food Chem. 51 (2003) 6036-6042.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 6036-6042
    • Doucet, D.1    Gauthier, S.F.2    Otter, D.3    Foegeding, E.A.4
  • 10
    • 84985154742 scopus 로고
    • Characterization of plastein reaction products formed by pepsin, a-chymotrypsin, and papain treatment of egg albumin hydrolysates
    • J. H. Edwards, W. F. Shipe, Characterization of plastein reaction products formed by pepsin, a-chymotrypsin, and papain treatment of egg albumin hydrolysates, J. Food Sci. 43 (4) (1978) 1215-1218.
    • (1978) J. Food Sci. , vol.43 , Issue.4 , pp. 1215-1218
    • Edwards, J.H.1    Shipe, W.F.2
  • 11
    • 84985070158 scopus 로고
    • The plastein reaction and its applications: A review
    • S. Eriksen, I. S. Fagerson, The plastein reaction and its applications: a review, J. Food Sci. 41 (3) (1976) 490-493.
    • (1976) J. Food Sci. , vol.41 , Issue.3 , pp. 490-493
    • Eriksen, S.1    Fagerson, I.S.2
  • 12
    • 31644441857 scopus 로고    scopus 로고
    • Enzymatic debittering of food protein hydrolysates
    • R. J. FitzGerald, G. O'Cuinn, Enzymatic debittering of food protein hydrolysates, Biotechnol. Adv. 24 (2) (2006) 234-237.
    • (2006) Biotechnol. Adv. , vol.24 , Issue.2 , pp. 234-237
    • FitzGerald, R.J.1    O'Cuinn, G.2
  • 13
    • 84926367537 scopus 로고
    • The apparent antigenicity of plastein
    • E. W. Flosdorf, S. Mudd, E. W. Flosdorf, The apparent antigenicity of plastein, J. Immunol. 32 (1937) 441-450.
    • (1937) J. Immunol. , vol.32 , pp. 441-450
    • Flosdorf, E.W.1    Mudd, S.2    Flosdorf, E.W.3
  • 14
    • 84926394914 scopus 로고
    • The nature of plastein
    • S. J. Folley, The nature of plastein, Biochem. J. 26 (1932) 99-105.
    • (1932) Biochem. J. , vol.26 , pp. 99-105
    • Folley, S.J.1
  • 15
    • 0002080621 scopus 로고
    • Enzymatic protein degradation and synthesis for protein improvement
    • M. Fujimaki, S. Arai, M. Yamashita, Enzymatic protein degradation and synthesis for protein improvement, Adv. Chem. Ser. 160 (1977) 156-184.
    • (1977) Adv. Chem. Ser. , vol.160 , pp. 156-184
    • Fujimaki, M.1    Arai, S.2    Yamashita, M.3
  • 16
    • 0015032152 scopus 로고
    • Application of microbial proteases to soybean and other materials to improve acceptability, especially through the formation of plastein
    • M. Fujimaki, H. Kato, S. Arai, M. Yamashita, Application of microbial proteases to soybean and other materials to improve acceptability, especially through the formation of plastein, J. Appl. Bacteriol. 34 (1) (1971) 119-131.
    • (1971) J. Appl. Bacteriol. , vol.34 , Issue.1 , pp. 119-131
    • Fujimaki, M.1    Kato, H.2    Arai, S.3    Yamashita, M.4
  • 17
    • 84996336978 scopus 로고
    • Enzymic modification of proteins in foodstuffs. I. Enzymic proteolysis and plastein synthesis application for preparing bland protein-like substrance
    • M. Fujimaki, M. Yamashita, S. Arai, H. Kato, Enzymic modification of proteins in foodstuffs. I. Enzymic proteolysis and plastein synthesis application for preparing bland protein-like substrance, Agric. Biol. Chem. 34 (9) (1970) 1325-1332.
    • (1970) Agric. Biol. Chem. , vol.34 , Issue.9 , pp. 1325-1332
    • Fujimaki, M.1    Yamashita, M.2    Arai, S.3    Kato, H.4
  • 18
    • 84865526599 scopus 로고    scopus 로고
    • Modification of soybean protein hydrolysates by alcalasecatalyzed plastein reaction and the ACE-inhibitory activity of the modified product in vitro
    • B. Gao, X. H. Zhao, Modification of soybean protein hydrolysates by alcalasecatalyzed plastein reaction and the ACE-inhibitory activity of the modified product in vitro, Int. J. Food Prop. 15 (5) (2012) 982-996.
    • (2012) Int. J. Food Prop. , vol.15 , Issue.5 , pp. 982-996
    • Gao, B.1    Zhao, X.H.2
  • 19
    • 0042134708 scopus 로고    scopus 로고
    • Peptide synthesis during in vitro proteolysis-transpeptidation or condensation?
    • A. Goepfert, P. C. Lorenzen, E. Schlimme, Peptide synthesis during in vitro proteolysis-transpeptidation or condensation? Food/Nahrung 43 (3) (1999) 211-212.
    • (1999) Food/Nahrung , vol.43 , Issue.3 , pp. 211-212
    • Goepfert, A.1    Lorenzen, P.C.2    Schlimme, E.3
  • 20
    • 45949122471 scopus 로고
    • Effects of nonprotein substances on protein hydrolysis and plastein formation
    • R. C. Hagan, R. Villota, Effects of nonprotein substances on protein hydrolysis and plastein formation, Food Chem. 23 (4) (1987) 277-294.
    • (1987) Food Chem. , vol.23 , Issue.4 , pp. 277-294
    • Hagan, R.C.1    Villota, R.2
  • 21
    • 84986522814 scopus 로고
    • The formation of heat and enzyme induced (plastein) gels from pepsin-hydrolyzed soy protein isolate
    • E. K. Hartnett, L. D. Satterlee, The formation of heat and enzyme induced (plastein) gels from pepsin-hydrolyzed soy protein isolate, J. Food Biochem. 14 (1) (1990) 1-13.
    • (1990) J. Food Biochem. , vol.14 , Issue.1 , pp. 1-13
    • Hartnett, E.K.1    Satterlee, L.D.2
  • 22
  • 23
    • 0042937798 scopus 로고
    • Production of protein hydrolysates and plastein from Alaska pollock
    • J. S. Hyung, H. Lee, Y. C. Hong, C. Y. Han, Production of protein hydrolysates and plastein from Alaska pollock, Korean Agric. Chem. Soc. 35 (5) (1992) 339-345.
    • (1992) Korean Agric. Chem. Soc. , vol.35 , Issue.5 , pp. 339-345
    • Hyung, J.S.1    Lee, H.2    Hong, Y.C.3    Han, C.Y.4
  • 24
    • 84926308628 scopus 로고
    • X-ray diagram of plastein
    • M. Kantola, A. I. Virtanen, X-ray diagram of plastein, Acta Chem. Scand. 4 (8) (1950) 1314-1315.
    • (1950) Acta Chem. Scand. , vol.4 , Issue.8 , pp. 1314-1315
    • Kantola, M.1    Virtanen, A.I.2
  • 25
    • 0042525336 scopus 로고
    • Plastein synthesis by a-chymotrypsin immobilized on hydrophobic agarose gel
    • I. Karube, Y. Yugeta, S. Suzuki, Plastein synthesis by a-chymotrypsin immobilized on hydrophobic agarose gel, J. Mol. Catal. 9 (4) (1980) 445-451.
    • (1980) J. Mol. Catal. , vol.9 , Issue.4 , pp. 445-451
    • Karube, I.1    Yugeta, Y.2    Suzuki, S.3
  • 26
    • 84988148041 scopus 로고
    • Effect of alkali halides on a-chymotrypsin activity in the plastein reaction
    • P. Lozano, D. Combes, Effect of alkali halides on a-chymotrypsin activity in the plastein reaction, J. Sci. Food Agric. 62 (3) (1993) 245-252.
    • (1993) J. Sci. Food Agric. , vol.62 , Issue.3 , pp. 245-252
    • Lozano, P.1    Combes, D.2
  • 27
    • 0141665548 scopus 로고
    • Papain-catalyzed synthesis of methionine-enriched soy plasteins. Average chain length of the plastein peptides
    • J. C. Monti, R. Jost, Papain-catalyzed synthesis of methionine-enriched soy plasteins. Average chain length of the plastein peptides, J. Agric. Food Chem. 27 (6) (1979) 1281-1285.
    • (1979) J. Agric. Food Chem. , vol.27 , Issue.6 , pp. 1281-1285
    • Monti, J.C.1    Jost, R.2
  • 28
    • 84926392040 scopus 로고
    • Plastein from pepsin and trypsin
    • J. H. Northrop, Plastein from pepsin and trypsin, J. Gen. Physiol. 30 (1947) 377-378.
    • (1947) J. Gen. Physiol. , vol.30 , pp. 377-378
    • Northrop, J.H.1
  • 29
    • 77956039862 scopus 로고    scopus 로고
    • Production of water soluble antioxidative plastein from squid hepatopancreas
    • S. Ono, D. Kasai, T. Sugano, K. Ohba, K. Takahashi, Production of water soluble antioxidative plastein from squid hepatopancreas, J. Oleo Sci. 53 (5) (2004) 267-273.
    • (2004) J. Oleo Sci. , vol.53 , Issue.5 , pp. 267-273
    • Ono, S.1    Kasai, D.2    Sugano, T.3    Ohba, K.4    Takahashi, K.5
  • 30
    • 0039935353 scopus 로고
    • Use of plastein reaction in recovering protein from fish waste
    • Y. Onoue, V. M. Riddle, Use of plastein reaction in recovering protein from fish waste, J. Fish. Board Can. 30 (11) (1973) 1745-1747.
    • (1973) J. Fish. Board Can. , vol.30 , Issue.11 , pp. 1745-1747
    • Onoue, Y.1    Riddle, V.M.2
  • 32
    • 33845550440 scopus 로고
    • Comparative study of soybean plasteins synthesized with soluble and immobilized alpha-chymotrypsin
    • C. Pallavicini, A. D. B. Peruffo, J. W. Finley, Comparative study of soybean plasteins synthesized with soluble and immobilized alpha-chymotrypsin, J. Agric. Food Chem. 31 (4) (1983) 846-848.
    • (1983) J. Agric. Food Chem. , vol.31 , Issue.4 , pp. 846-848
    • Pallavicini, C.1    Peruffo, A.D.B.2    Finley, J.W.3
  • 33
    • 84986865527 scopus 로고
    • Synthesis of plasteins from fish silage
    • M. R. Raghunath, A. R. McCurdy, Synthesis of plasteins from fish silage, J. Sci. Food Agric. 54 (4) (1991) 655-658.
    • (1991) J. Sci. Food Agric. , vol.54 , Issue.4 , pp. 655-658
    • Raghunath, M.R.1    McCurdy, A.R.2
  • 34
    • 0034868610 scopus 로고    scopus 로고
    • Debittering of protein hydrolyzates
    • B. C. Saha, K. Hayashi, Debittering of protein hydrolyzates, Biotechnol. Adv. 19 (5) (2001) 355-370.
    • (2001) Biotechnol. Adv. , vol.19 , Issue.5 , pp. 355-370
    • Saha, B.C.1    Hayashi, K.2
  • 35
    • 84985348744 scopus 로고
    • Modification of leaf protein concentrate by the use of plastein reaction
    • V. A. Savangikar, R. N. Joshi, Modification of leaf protein concentrate by the use of plastein reaction, J. Sci. Food Agric. 30 (9) (1979) 899-905.
    • (1979) J. Sci. Food Agric. , vol.30 , Issue.9 , pp. 899-905
    • Savangikar, V.A.1    Joshi, R.N.2
  • 36
    • 0033180421 scopus 로고    scopus 로고
    • Use of NMR and mass spectrometry to detect and quantify protease-catalyzed peptide bond formation in complex mixtures
    • D. E. Stevenson, K. R. Morgan, G. A. Fenton, G. Moraes, Use of NMR and mass spectrometry to detect and quantify protease-catalyzed peptide bond formation in complex mixtures, Enzyme Microb. Technol. 25 (3) (1999) 357-363.
    • (1999) Enzyme Microb. Technol. , vol.25 , Issue.3 , pp. 357-363
    • Stevenson, D.E.1    Morgan, K.R.2    Fenton, G.A.3    Moraes, G.4
  • 37
    • 0032007918 scopus 로고    scopus 로고
    • Protease-catalyzed condensation of peptides as a potential means to reduce the bitter taste of hydrophobic peptides found in protein hydrolysates
    • D. E. Stevenson, D. J. Ofman, K. R. Morgan, R. A. Stanley, Protease-catalyzed condensation of peptides as a potential means to reduce the bitter taste of hydrophobic peptides found in protein hydrolysates, Enzyme Microb. Technol. 22 (1998) 100-110.
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 100-110
    • Stevenson, D.E.1    Ofman, D.J.2    Morgan, K.R.3    Stanley, R.A.4
  • 38
    • 84974224136 scopus 로고
    • Application of the plastein reaction to caseins and to skim-milk powder: I. Protein hydrolysis and plastein formation
    • G. Sukan, A. T. Andrews, Application of the plastein reaction to caseins and to skim-milk powder: I. Protein hydrolysis and plastein formation, J. Dairy Res. 49 (2) (1982) 265-278.
    • (1982) J. Dairy Res. , vol.49 , Issue.2 , 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 and the mechanism of plastein formation
    • G. Sukan, A. T. Andrews, Application of the plastein reaction to caseins and to skim-milk powder: II. Chemical and physical properties of the plasteins and the mechanism of plastein formation, J. Dairy Res. 49 (1982) 279-293.
    • (1982) J. Dairy Res. , vol.49 , pp. 279-293
    • Sukan, G.1    Andrews, A.T.2
  • 40
    • 84862784553 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme inhibition and enzymatic resistance in vitro of casein hydrolysate treated by plastein reaction and fractionated with ethanol/water or methanol/water
    • H. Sun, X. H. Zhao, Angiotensin I converting enzyme inhibition and enzymatic resistance in vitro of casein hydrolysate treated by plastein reaction and fractionated with ethanol/water or methanol/water, Int. Dairy J. 24 (1) (2012) 27-32.
    • (2012) Int. Dairy J. , vol.24 , Issue.1 , pp. 27-32
    • Sun, H.1    Zhao, X.H.2
  • 41
    • 0030298543 scopus 로고    scopus 로고
    • Preparation of hydrolysates from bovine red blood cells and their debittering following plastein reaction
    • J. Synowiecki, R. Jagietka, F. Shahidi, Preparation of hydrolysates from bovine red blood cells and their debittering following plastein reaction, Food Chem. 57 (3) (1996) 435-439.
    • (1996) Food Chem. , vol.57 , Issue.3 , pp. 435-439
    • Synowiecki, J.1    Jagietka, R.2    Shahidi, F.3
  • 42
    • 38249011722 scopus 로고
    • Supplemental effects of methionineenriched plastein in Penaeus japonicas diets
    • S. Teshima, A. Kanazawa, S. Koshio, Supplemental effects of methionineenriched plastein in Penaeus japonicas diets, Aquaculture 101 (1) (1992) 85-93.
    • (1992) Aquaculture , vol.101 , Issue.1 , pp. 85-93
    • Teshima, S.1    Kanazawa, A.2    Koshio, S.3
  • 43
    • 84872882776 scopus 로고
    • Effect of substrate concentration on plastein productivity and some rheological properties of the products
    • S.-J. Tsai, M. Yamashita, S. Arai, M. Fujimaki, Effect of substrate concentration on plastein productivity and some rheological properties of the products, Agr. Biol. Chem. 36 (1972) 1045.
    • (1972) Agr. Biol. Chem. , vol.36 , pp. 1045
    • Tsai, S.-J.1    Yamashita, M.2    Arai, S.3    Fujimaki, M.4
  • 44
    • 84897110510 scopus 로고    scopus 로고
    • Bioinformatics approaches, prospects and challenges of food bioactive peptide research
    • C. C. Udenigwe, Bioinformatics approaches, prospects and challenges of food bioactive peptide research, Trends Food Sci. Technol. 36 (2) (2014) 137-143.
    • (2014) Trends Food Sci. Technol. , vol.36 , Issue.2 , pp. 137-143
    • Udenigwe, C.C.1
  • 45
    • 84856032752 scopus 로고    scopus 로고
    • Food protein-derived bioactive peptides: Production, processing, and potential health benefits
    • C. C. Udenigwe, R. E. Aluko, Food protein-derived bioactive peptides: production, processing, and potential health benefits, J. Food Sci. 77 (1) (2012) R11-R24.
    • (2012) J. Food Sci. , vol.77 , Issue.1 , pp. R11-R24
    • Udenigwe, C.C.1    Aluko, R.E.2
  • 46
    • 84892164302 scopus 로고    scopus 로고
    • Revisiting the prospects of plastein: Thermal and simulated gastric stability in relation to the antioxidative capacity of casein plastein
    • C. C. Udenigwe, S. Wu, K. Drummond, M. Gong, Revisiting the prospects of plastein: thermal and simulated gastric stability in relation to the antioxidative capacity of casein plastein, J. Agric. Food Chem. 62 (1) (2014) 130-135.
    • (2014) J. Agric. Food Chem. , vol.62 , Issue.1 , pp. 130-135
    • Udenigwe, C.C.1    Wu, S.2    Drummond, K.3    Gong, M.4
  • 47
    • 0016956753 scopus 로고
    • Protease-catalyzed formation of plastein products and some of their properties
    • B. Van Hofsten, G. Lalasidis, Protease-catalyzed formation of plastein products and some of their properties, J. Agric. Food Chem. 24 (1976) 460-465.
    • (1976) J. Agric. Food Chem. , vol.24 , pp. 460-465
    • Van Hofsten, B.1    Lalasidis, G.2
  • 48
    • 84926362106 scopus 로고
    • Obesrvations on the formation and structure of pla3
    • A. I. Virtanen, H. K. Kerkkonen, T. Laaksonen, Obesrvations on the formation and structure of pla3, Acta Chem. Scand. 2 (10) (1948) 933-935.
    • (1948) Acta Chem. Scand. , vol.2 , Issue.10 , pp. 933-935
    • Virtanen, A.I.1    Kerkkonen, H.K.2    Laaksonen, T.3
  • 49
    • 77649208099 scopus 로고
    • The enzymatic synthesis of protein. II. The effect of temperature on the synthesizing action of pepsin
    • H. Wasteneys, H. Borsook, The enzymatic synthesis of protein. II. The effect of temperature on the synthesizing action of pepsin, J. Biol. Chem. 62 (1924) 15-29.
    • (1924) J. Biol. Chem. , vol.62 , pp. 15-29
    • Wasteneys, H.1    Borsook, H.2
  • 50
    • 0041011763 scopus 로고
    • The enzymatic synthesis of protein
    • H. Wasteneys, H. Borsook, The enzymatic synthesis of protein, Physiol. Rev. 10 (1930) 110-145.
    • (1930) Physiol. Rev. , vol.10 , pp. 110-145
    • Wasteneys, H.1    Borsook, H.2
  • 51
    • 0035132362 scopus 로고    scopus 로고
    • Application of the plastein reaction to mycoprotein: I. Plastein synthesis
    • R. J. H. Williams, V. L. Brownsell, A. T. Andrews, Application of the plastein reaction to mycoprotein: I. Plastein synthesis, Food Chem. 72 (3) (2001) 329-335.
    • (2001) Food Chem. , vol.72 , Issue.3 , pp. 329-335
    • Williams, R.J.H.1    Brownsell, V.L.2    Andrews, A.T.3
  • 52
    • 84897655686 scopus 로고    scopus 로고
    • Optimization of some conditions of neutrasecatalyzed plastein reaction to mediate ACE-inhibitory activity in vitro of casein hydrolysate prepared by Neutrase
    • W. Xu, B. H. Kong, X. H. Zhao, Optimization of some conditions of neutrasecatalyzed plastein reaction to mediate ACE-inhibitory activity in vitro of casein hydrolysate prepared by Neutrase, Food Sci. Technol. 51 (2) (2014) 276-284.
    • (2014) Food Sci. Technol. , vol.51 , Issue.2 , pp. 276-284
    • Xu, W.1    Kong, B.H.2    Zhao, X.H.3
  • 53
    • 0015868836 scopus 로고
    • Condensation reaction occurring during plastein formation by a-chymotrypsin
    • M. Yamashita, S. Arai, S. Tanimoto, et al., Condensation reaction occurring during plastein formation by a-chymotrypsin, Agric. Biol. Chem. 37 (4) (1973) 953-954.
    • (1973) Agric. Biol. Chem. , vol.37 , Issue.4 , pp. 953-954
    • Yamashita, M.1    Arai, S.2    Tanimoto, S.3
  • 54
    • 33847799978 scopus 로고
    • Plastein reaction for food protein improvement
    • M. Yamashita, S. Arai, M. Fujimaki, Plastein reaction for food protein improvement, J. Agric. Food Chem. 24 (6) (1976) 1100-1104.
    • (1976) J. Agric. Food Chem. , vol.24 , Issue.6 , pp. 1100-1104
    • Yamashita, M.1    Arai, S.2    Fujimaki, M.3
  • 55
    • 0011916568 scopus 로고
    • Synthesis and characterization of a glutamic acid enriched plastein with greater solubility
    • M. Yamashita, S. Arai, S. Kokubo, K. Aso, M. Fujimaki, Synthesis and characterization of a glutamic acid enriched plastein with greater solubility, J. Agric. Food Chem. 23 (1) (1975) 27-30.
    • (1975) J. Agric. Food Chem. , vol.23 , Issue.1 , pp. 27-30
    • Yamashita, M.1    Arai, S.2    Kokubo, S.3    Aso, K.4    Fujimaki, M.5
  • 56
    • 85008293067 scopus 로고
    • Supplementing sulfur-containing amino acids by plastein reaction
    • M. Yamashita, S. Arai, S. J. Tsai, M. Fujimaki, Supplementing sulfur-containing amino acids by plastein reaction, Agric. Biol. Chem. 34 (10) (1970) 1593-1596.
    • (1970) Agric. Biol. Chem. , vol.34 , Issue.10 , pp. 1593-1596
    • Yamashita, M.1    Arai, S.2    Tsai, S.J.3    Fujimaki, M.4
  • 57
    • 0015148275 scopus 로고
    • Plastein reaction as a method for enhancing the sulfur-containing amino acid level of soybean protein
    • M. Yamashita, S. Arai, S.-J. Tsai, M. Fujimaki, Plastein reaction as a method for enhancing the sulfur-containing amino acid level of soybean protein, J. Agric. Food Chem. 19 (1971) 1151T.
    • (1971) J. Agric. Food Chem. , vol.19 , pp. 1151T
    • Yamashita, M.1    Arai, S.2    Tsai, S.-J.3    Fujimaki, M.4
  • 59
    • 84901825023 scopus 로고    scopus 로고
    • In vitro calcium-chelating and platelet anti-aggregation activities of soy protein hydrolysate modified by the alcalase-catalyzed plastein reaction
    • M. L. Zhang, X. H. Zhao, In vitro calcium-chelating and platelet anti-aggregation activities of soy protein hydrolysate modified by the alcalase-catalyzed plastein reaction, J. Food Biochem. 38 (3) (2014) 374-380.
    • (2014) J. Food Biochem. , vol.38 , Issue.3 , pp. 374-380
    • Zhang, M.L.1    Zhao, X.H.2
  • 60
    • 70349986477 scopus 로고    scopus 로고
    • An approach to improve ACE-inhibitory activity of casein hydrolysates with plastein reaction catalyzed by alcalase
    • X. H. Zhao, Y. Y. Li, An approach to improve ACE-inhibitory activity of casein hydrolysates with plastein reaction catalyzed by alcalase, Eur. Food Res. Technol. 229 (5) (2009) 795-805.
    • (2009) Eur. Food Res. Technol. , vol.229 , Issue.5 , pp. 795-805
    • Zhao, X.H.1    Li, Y.Y.2
  • 61
    • 84896933050 scopus 로고    scopus 로고
    • In vitro cytoprotection of modified casein hydrolysates by plastein reaction on rat hepatocyte cells
    • X. H. Zhao, Y. Fu, N. Yue, In vitro cytoprotection of modified casein hydrolysates by plastein reaction on rat hepatocyte cells, CyTA-J. Food 12 (1) (2014) 40-47.
    • (2014) CyTA-J. Food , vol.12 , Issue.1 , pp. 40-47
    • Zhao, X.H.1    Fu, Y.2    Yue, N.3
  • 62
    • 77956048282 scopus 로고    scopus 로고
    • Preparation and radical scavenging activity of papain-catalyzed casein plasteins
    • X. H. Zhao, D. Wu, T. J. Li, Preparation and radical scavenging activity of papain-catalyzed casein plasteins, Dairy Sci. Technol. 90 (5) (2010) 521-535.
    • (2010) Dairy Sci. Technol. , vol.90 , Issue.5 , pp. 521-535
    • Zhao, X.H.1    Wu, D.2    Li, T.J.3


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