메뉴 건너뛰기




Volumn 6, Issue 9, 2006, Pages 1087-1101

Effect of limited hydrolysis on traditional soy protein concentrate

Author keywords

Extractability; Limited hydrolysis; Phytic acid; Protein composition; Soy protein concentrate; Trypsin inhibitor activity

Indexed keywords

ELECTROPHORESIS; EMULSIFICATION; HYDROLYSIS; PROTEOLYSIS;

EID: 33749564789     PISSN: 14243210     EISSN: 14248220     Source Type: Journal    
DOI: 10.3390/s6091087     Document Type: Article
Times cited : (28)

References (41)
  • 1
    • 84907421527 scopus 로고
    • Effect of thermal treatment soy protein isolate on the characteristics and structure- Function relationship of soluble and insoluble fractions
    • Sorgentini, A. D.; Wagner, J. R.; Anon, M. C. Effect of thermal treatment soy protein isolate on the characteristics and structure- function relationship of soluble and insoluble fractions. J. Agric. Food Chem. 1995, 43, 2471-2479.
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 2471-2479
    • Sorgentini, A.D.1    Wagner, J.R.2    Anon, M.C.3
  • 3
    • 0000678633 scopus 로고
    • Physicochemical and functional properties of oilseed proteins with emphasis on soy proteins
    • Altschul, A.M., Wilke, H.L. eds., Academic Press: New York
    • Kinsella, J. E.; German,B.; Damodoran, S. Physicochemical and functional properties of oilseed proteins with emphasis on soy proteins. In New Protein Foods, Altschul, A.M., Wilke, H.L. eds., Academic Press: New York, 1985, Vol. 5, pp107-179.
    • (1985) New Protein Foods , vol.5 , pp. 107-179
    • Kinsella, J.E.1    German, B.2    Damodoran, S.3
  • 4
    • 51249180057 scopus 로고
    • Functional properties of soy proteins
    • Kinsella, J. E. Functional properties of soy proteins. J. Am. Oil Chem. Soc. 1979, 56, 242-258.
    • (1979) J. Am. Oil Chem. Soc. , vol.56 , pp. 242-258
    • Kinsella, J.E.1
  • 5
    • 0002787444 scopus 로고
    • Functionality of soy proteins
    • Hettiarachchy, N. S., Ziegler, G. R. eds., Dekker, New York
    • Rhee, K. C. Functionality of soy proteins. In Protein Functionality in Food Systems Hettiarachchy, N. S., Ziegler, G. R. eds., Dekker, New York, 1994, pp311-324.
    • (1994) Protein Functionality in Food Systems , pp. 311-324
    • Rhee, K.C.1
  • 6
    • 0023565542 scopus 로고
    • Specific limited hudrolysis and phosphorylation of food proteins for improvement of functional and nutritional properties
    • Chobert, J. M; Sitohy, M.Z.; Whitaker, D. J.R. Specific limited hudrolysis and phosphorylation of food proteins for improvement of functional and nutritional properties, J.Am. Oil Chem. Soc. 1987, 36, 1704-1711.
    • (1987) J.Am. Oil Chem. Soc. , vol.36 , pp. 1704-1711
    • Chobert, J.M.1    Sitohy, M.Z.2    Whitaker, D.J.R.3
  • 7
    • 84907421510 scopus 로고
    • The relationship between the method of obtention and the structural and functional properties of soy protein isolates 1. Structural and hydration properties
    • Petrucelli, S.; Anon, M. C. The relationship between the method of obtention and the structural and functional properties of soy protein isolates 1. Structural and hydration properties. J. Agric. Food Chem. 1994a, 42, 2161-2169.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 2161-2169
    • Petrucelli, S.1    Anon, M.C.2
  • 8
    • 84907421519 scopus 로고
    • The relationship between the method of obtention and the strustural and functional properties of soy protein isolates 2. Surface properties
    • Petrucelli, S.; Anon, M. C. The relationship between the method of obtention and the strustural and functional properties of soy protein isolates 2. Surface properties. J. Agric. Food Chem. 1994b, 42, 2170-2176.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 2170-2176
    • Petrucelli, S.1    Anon, M.C.2
  • 9
    • 0001642128 scopus 로고
    • Influence of denaturation degree, hydrophobicity and sulphydryl content on solubility and water absorbing capacity of soy protein isolates
    • Wagner, J. R.; Anon, M. C. Influence of denaturation degree, hydrophobicity and sulphydryl content on solubility and water absorbing capacity of soy protein isolates, J. Agric. Food Chem. 1990, 50, 765-770.
    • (1990) J. Agric. Food Chem. , vol.50 , pp. 765-770
    • Wagner, J.R.1    Anon, M.C.2
  • 10
    • 84907421537 scopus 로고
    • Electrophoretic, solubility, and functional properties of commercial soy protein isolates
    • Arrese, E.L.; Sorgentini, D. A.; Wagner,.J.R.; Annon, M.C. Electrophoretic, solubility, and functional properties of commercial soy protein isolates, J. Agric. Food Chem. 1991, 39, 1029-1032.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 1029-1032
    • Arrese, E.L.1    Sorgentini, D.A.2    Wagner, J.R.3    Annon, M.C.4
  • 11
    • 0033852356 scopus 로고    scopus 로고
    • Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory-prepared soy protein isolates
    • Wagner, J. R.; Sorgentini, D. A; Anon M. C. Relation between solubility and surface hydrophobicity as an indicator of modifications during preparation processes of commercial and laboratory-prepared soy protein isolates, J. Agric. Food Chem. 2000, 48, 3159-3165.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 3159-3165
    • Wagner, J.R.1    Sorgentini, D.A.2    Anon, M.C.3
  • 12
    • 0000617029 scopus 로고
    • Functional properties of proteolytic enzyme modified soy protein isolate
    • Kim, S.Y.; Park, P.S.W.; Rhee, K.C. Functional properties of proteolytic enzyme modified soy protein isolate, J. Agric. Food Chem. 1990, 33, 651-656.
    • (1990) J. Agric. Food Chem. , vol.33 , pp. 651-656
    • Kim, S.Y.1    Park, P.S.W.2    Rhee, K.C.3
  • 15
    • 15444361602 scopus 로고    scopus 로고
    • In vitro accessibility of untreated, toasted and extruded soybean meals for proteases and carbohydrases
    • Were, L.; Hettiarachchy, N. S.; Kalapathy, U. In vitro accessibility of untreated, toasted and extruded soybean meals for proteases and carbohydrases. J. Food Sci., 1997, 62, 821-823.
    • (1997) J. Food Sci. , vol.62 , pp. 821-823
    • Were, L.1    Hettiarachchy, N.S.2    Kalapathy, U.3
  • 16
    • 0342804403 scopus 로고    scopus 로고
    • Enzymatic hydrolysis and synthesis of soy protein to improve its amino acid composition and functional properties
    • Calderon de la Barca, A. M.; Ruiz-Salazar, R. A.; Jara-Marini, M. E. Enzymatic hydrolysis and synthesis of soy protein to improve its amino acid composition and functional properties. J. Food Sci. 2000, 65, 246-253.
    • (2000) J. Food Sci. , vol.65 , pp. 246-253
    • Calderon De La Barca, A.M.1    Ruiz-Salazar, R.A.2    Jara-Marini, M.E.3
  • 17
    • 0036392199 scopus 로고    scopus 로고
    • Hydrolysates of native and modified soy protein isolates: Structural characteristics, solubility and foaming properties
    • Molina Ortiz, S.E.; Wagner, J.R. Hydrolysates of native and modified soy protein isolates: structural characteristics, solubility and foaming properties, Food Res. Int. 2002, 35, 511-518.
    • (2002) Food Res. Int. , vol.35 , pp. 511-518
    • Molina Ortiz, S.E.1    Wagner, J.R.2
  • 18
    • 1542304014 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of defatted soy four by three different proteases and their effect on the functional properties of resulting protein hydrolysates
    • Hrackova, M.; Rusnakova, M.; Zemanovic, J. Enzymatic hydrolysis of defatted soy four by three different proteases and their effect on the functional properties of resulting protein hydrolysates. Czech Journal of Food Science 2002, 20, 7-14.
    • (2002) Czech Journal of Food Science , vol.20 , pp. 7-14
    • Hrackova, M.1    Rusnakova, M.2    Zemanovic, J.3
  • 19
    • 0032446301 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of soy protein isolate and effect of succinylation on the functional properties of resulting hydrolysates
    • Achouri, A.; Zhang, W.; Xu, S. Enzymatic hydrolysis of soy protein isolate and effect of succinylation on the functional properties of resulting hydrolysates. Food Res. Int. 1998, 31, 617-623.
    • (1998) Food Res. Int. , vol.31 , pp. 617-623
    • Achouri, A.1    Zhang, W.2    Xu, S.3
  • 20
    • 0034992888 scopus 로고    scopus 로고
    • Effect of succinylation on the physicochemical properties of soy protein hydrolysate
    • Achouri, A.; Zhang, W. Effect of succinylation on the physicochemical properties of soy protein hydrolysate, Food Res. Int., 2001, 56, 507-514.
    • (2001) Food Res. Int. , vol.56 , pp. 507-514
    • Achouri, A.1    Zhang, W.2
  • 21
    • 0037205616 scopus 로고    scopus 로고
    • Aggregation of peptides during hydrolysis as a cause of reduced enzymatic extractability of soybean meal proteins
    • Fischer, M.; Gruppen, H.; Piersma, S. R.; Kofod, L. V.; Schols, H. A.; Voragen, A. G. J. Aggregation of peptides during hydrolysis as a cause of reduced enzymatic extractability of soybean meal proteins, J. Agric. Food Chem. 2002, 50, 4512-4519.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 4512-4519
    • Fischer, M.1    Gruppen, H.2    Piersma, S.R.3    Kofod, L.V.4    Schols, H.A.5    Voragen, A.G.J.6
  • 23
    • 0017019007 scopus 로고
    • Major proteins of soybean seeds. A straightforward fractionation and their characterization
    • Thanh, V. H.; Shibasaki, K. Major proteins of soybean seeds. A straightforward fractionation and their characterization. J. Agric. Food Chem. 1976, 24, 1117-1121.
    • (1976) J. Agric. Food Chem. , vol.24 , pp. 1117-1121
    • Thanh, V.H.1    Shibasaki, K.2
  • 25
    • 78651153791 scopus 로고
    • Disc electrophoresis- II Method and application to human serum proteins
    • Davis, J. Disc Electrophoresis- II Method and application to human serum proteins, Annals N. Y. Ac. Sci.1964, 121, 404-427.
    • (1964) Annals N. Y. Ac. Sci. , vol.121 , pp. 404-427
    • Davis, J.1
  • 26
    • 0022539027 scopus 로고
    • Peptide and protein molecular weight determination by electrophoresis using a high-molarity Tris- Buffer system without urea
    • Fling, S. P.; Gregerson, D. S. Peptide and protein molecular weight determination by electrophoresis using a high-molarity Tris- buffer system without urea. Anal. Biochem. 1986, 155, 83-88.
    • (1986) Anal. Biochem. , vol.155 , pp. 83-88
    • Fling, S.P.1    Gregerson, D.S.2
  • 27
    • 0032116216 scopus 로고    scopus 로고
    • Hydrophobicity, solubility, and emulsifying of soy protein prepared by papain modification and ultrafiltration
    • Wu, W. U.; Hettiararchy, N. S.; Qui, M. Hydrophobicity, solubility, and emulsifying of soy protein prepared by papain modification and ultrafiltration. J.Am. Oil Chem. Soc. 1998, 75, 845-850.
    • (1998) J.Am. Oil Chem. Soc. , vol.75 , pp. 845-850
    • Wu, W.U.1    Hettiararchy, N.S.2    Qui, M.3
  • 28
    • 0000367867 scopus 로고
    • An improved colorimetric method for determination antitryptic activity in soybean products
    • Liu, M.; Markakis, P. An improved colorimetric method for determination antitryptic activity in soybean products. Cereal Chem. 1989, 66, 415-421.
    • (1989) Cereal Chem. , vol.66 , pp. 415-421
    • Liu, M.1    Markakis, P.2
  • 29
    • 84986532481 scopus 로고
    • Phytic acid determination in soybeans
    • Thomson, D.B.; Erdman, J. W. Phytic acid determination in soybeans. J.Food Sci. 1982, 47, 513-519.
    • (1982) J.Food Sci. , vol.47 , pp. 513-519
    • Thomson, D.B.1    Erdman, J.W.2
  • 31
    • 17744383239 scopus 로고    scopus 로고
    • The effect of microwave roasting on soybean protein composition and components with trypsin inhibitor activity
    • Barac, M., Stanojevic, S. The effect of microwave roasting on soybean protein composition and components with trypsin inhibitor activity, Acta Alimentaria, 2005, 34, 23-31.
    • (2005) Acta Alimentaria , vol.34 , pp. 23-31
    • Barac, M.1    Stanojevic, S.2
  • 32
    • 0032168087 scopus 로고    scopus 로고
    • Imunochemical examination of the surface physico-chemical properties of various dicotyledonous and monocotyledonous globulin seed storage proteins
    • Marcone, M.F.; Kakuda, Y.; Yada R.Y. Imunochemical examination of the surface physico-chemical properties of various dicotyledonous and monocotyledonous globulin seed storage proteins, Food Chem. 1998, 63, 85-95.
    • (1998) Food Chem. , vol.63 , pp. 85-95
    • Marcone, M.F.1    Kakuda, Y.2    Yada, R.Y.3
  • 34
    • 0021892941 scopus 로고
    • Glycinin A3B4 mRNA: Cloning and sequencing of double stranded cDNA complementary to a soybean storage protein
    • Fukazawa, C.; Momma, T.; Hirano, H.; Harada, K.; Udaka,K. Glycinin A3B4 mRNA: cloning and sequencing of double stranded cDNA complementary to a soybean storage protein, J. Biol. Chem. 1985, 260, 6234-6239.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6234-6239
    • Fukazawa, C.1    Momma, T.2    Hirano, H.3    Harada, K.4    Udaka, K.5
  • 35
    • 0343725673 scopus 로고    scopus 로고
    • Analysis of products, mechanisms of reaction, and some functional properties of soy protein hydrolysates
    • Molina Ortiz, S.E.; Anon, M.C. Analysis of products, mechanisms of reaction, and some functional properties of soy protein hydrolysates, J. Am.Oil Chem. Soc. 2000, 77, 1293-1302.
    • (2000) J. Am.Oil Chem. Soc. , vol.77 , pp. 1293-1302
    • Molina Ortiz, S.E.1    Anon, M.C.2
  • 36
    • 0019331914 scopus 로고
    • Hydrophobicity determined by fluorescence probe method and its correlation with surface properties of proteins
    • Kato, A. and S. Nakai Hydrophobicity Determined by Fluorescence probe Method and Its Correlation with Surface Properties of Proteins, Biochim.Biophys.Acta 1980, 624, 13-20.
    • (1980) Biochim.Biophys.Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 37
    • 33845550183 scopus 로고
    • Structure-functional relationship of food proteins with emphasis on the importance of the protein hydrophobidty
    • Nakai, S. Structure-Functional Relationship of Food Proteins with Emphasis on the Importance of the Protein Hydrophobidty,J.Agric.Food Chem. 1983, 31, 676-683.
    • (1983) J.Agric.Food Chem. , vol.31 , pp. 676-683
    • Nakai, S.1
  • 38
    • 33749556860 scopus 로고    scopus 로고
    • The influence of genotypic variation in protein composition on emulsifying properties of soy proteins
    • Pesic, M.; Vucelic-Radovic, B.; Barac, M.; Stanojevic, S. The Influence of Genotypic Variation in Protein Composition on Emulsifying Properties of Soy Proteins, J.Am.Oil.Chem. 2005, 82(9), 667-672.
    • (2005) J.Am.Oil.Chem. , vol.82 , Issue.9 , pp. 667-672
    • Pesic, M.1    Vucelic-Radovic, B.2    Barac, M.3    Stanojevic, S.4
  • 39
    • 0034958041 scopus 로고    scopus 로고
    • Bowman-Birk inhibitors in soybean seed coats
    • Sessa, D. J.; Wolf, W.J. Bowman-Birk inhibitors in soybean seed coats. Ind. Crops Prod. 2001, 14, 73-83.
    • (2001) Ind. Crops Prod. , vol.14 , pp. 73-83
    • Sessa, D.J.1    Wolf, W.J.2
  • 40
    • 0023559604 scopus 로고
    • Reduction of phytic acid concentration in protein isolates by acylation techniques
    • Thomson, L. Reduction of phytic acid concentration in protein isolates by acylation techniques. J. Am. Oil. Chem. Soc 1987, 64, 1712.
    • (1987) J. Am. Oil. Chem. Soc , vol.64 , pp. 1712
    • Thomson, L.1
  • 41
    • 0041623460 scopus 로고    scopus 로고
    • Phytochemicals in soybean - Their potential helth benefits
    • Wang, C.; Wixon, R. Phytochemicals in soybean - Their potential helth benefits, Inform 1999, 10, 315-320.
    • (1999) Inform , vol.10 , pp. 315-320
    • Wang, C.1    Wixon, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.