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Volumn 23, Issue 3, 2009, Pages 936-941

Interactions between whey soybean protein (WSP) and beta-conglycinin (7S) during the formation of protein particles at elevated temperatures

Author keywords

Beta conglycinin (7S); Heat treatment; Protein particle formation; Soymilk; Whey soybean protein (WSP)

Indexed keywords

GLYCINE MAX;

EID: 54249125343     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2008.06.007     Document Type: Article
Times cited : (30)

References (29)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72 (1976) 248-254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 0001614419 scopus 로고
    • Effect of β-conglycinin on the thermal aggregation of glycinin
    • Damodaran S., and Kinsella J.E. Effect of β-conglycinin on the thermal aggregation of glycinin. Journal of Agricultural & Food Chemistry 30 5 (1982) 812-817
    • (1982) Journal of Agricultural & Food Chemistry , vol.30 , Issue.5 , pp. 812-817
    • Damodaran, S.1    Kinsella, J.E.2
  • 4
    • 19444376562 scopus 로고    scopus 로고
    • The role of composition and content of protein particles in soymilk on the tofu curding by glucono-δ-lactone or calcium sulfate
    • Guo S.T., and Ono T. The role of composition and content of protein particles in soymilk on the tofu curding by glucono-δ-lactone or calcium sulfate. Journal of Food Science 70 4 (2005) c258-c262
    • (2005) Journal of Food Science , vol.70 , Issue.4
    • Guo, S.T.1    Ono, T.2
  • 5
    • 0012168405 scopus 로고    scopus 로고
    • Interaction between protein and lipid in soybean milk at elevated temperature
    • Guo S.T., Ono T., and Mikami M. Interaction between protein and lipid in soybean milk at elevated temperature. Journal of Agricultural & Food Chemistry 45 12 (1997) 4601-4605
    • (1997) Journal of Agricultural & Food Chemistry , vol.45 , Issue.12 , pp. 4601-4605
    • Guo, S.T.1    Ono, T.2    Mikami, M.3
  • 6
    • 0000316158 scopus 로고
    • Electrophoretic analysis of whey proteins present in soybean globulin fractions
    • Iwabuchi S., and Yamauchi F. Electrophoretic analysis of whey proteins present in soybean globulin fractions. Journal of Agricultural & Food Chemistry 35 2 (1987) 205-209
    • (1987) Journal of Agricultural & Food Chemistry , vol.35 , Issue.2 , pp. 205-209
    • Iwabuchi, S.1    Yamauchi, F.2
  • 7
    • 0019542905 scopus 로고
    • 2S globulins of soybean seeds. II. Physicochemical and biological properties of protease inhibitors in 2S globulins
    • Koshiyama I., Kikuchi M., and Fukushima D. 2S globulins of soybean seeds. II. Physicochemical and biological properties of protease inhibitors in 2S globulins. Journal of Agricultural & Food Chemistry 29 2 (1981) 340-343
    • (1981) Journal of Agricultural & Food Chemistry , vol.29 , Issue.2 , pp. 340-343
    • Koshiyama, I.1    Kikuchi, M.2    Fukushima, D.3
  • 8
    • 33751583648 scopus 로고    scopus 로고
    • Opposite contributions of glycinin- and β-conglycinin-derived peptides to the aggregation behavior of soy protein isolate hydrolysates
    • Kuipers B.J.H., Koningsveld G.A.V., Alting A.C., Driehuis F., Voragen A.G.J., and Gruppen H. Opposite contributions of glycinin- and β-conglycinin-derived peptides to the aggregation behavior of soy protein isolate hydrolysates. Food Biophysics 1 (2006) 178-188
    • (2006) Food Biophysics , vol.1 , pp. 178-188
    • Kuipers, B.J.H.1    Koningsveld, G.A.V.2    Alting, A.C.3    Driehuis, F.4    Voragen, A.G.J.5    Gruppen, H.6
  • 9
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 10
    • 0000174052 scopus 로고
    • LOX inactivation by manothermosonication: effects of sonication physical parameters, pH, KCl, sugars, glycerol, and enzyme concentration
    • Lopez P., and Burgos J. LOX inactivation by manothermosonication: effects of sonication physical parameters, pH, KCl, sugars, glycerol, and enzyme concentration. Journal of Agricultural & Food Chemistry 43 3 (1995) 620-625
    • (1995) Journal of Agricultural & Food Chemistry , vol.43 , Issue.3 , pp. 620-625
    • Lopez, P.1    Burgos, J.2
  • 16
    • 85007708549 scopus 로고
    • Changes in the composition and size distribution of soymilk protein particles by heating
    • Ono T., Choi M.R., Ikeda A., and Odagiri S. Changes in the composition and size distribution of soymilk protein particles by heating. Agricultural & Biological Chemistry 55 9 (1991) 2291-2297
    • (1991) Agricultural & Biological Chemistry , vol.55 , Issue.9 , pp. 2291-2297
    • Ono, T.1    Choi, M.R.2    Ikeda, A.3    Odagiri, S.4
  • 17
    • 0001834669 scopus 로고
    • Influences of calcium and pH on protein solubility in soybean milk
    • Ono T., Katho S., and Mothizuki K. Influences of calcium and pH on protein solubility in soybean milk. Bioscience Biotechnology & Biochemistry 57 1 (1993) 24-28
    • (1993) Bioscience Biotechnology & Biochemistry , vol.57 , Issue.1 , pp. 24-28
    • Ono, T.1    Katho, S.2    Mothizuki, K.3
  • 18
    • 0029987403 scopus 로고    scopus 로고
    • Interaction of protein particles with lipids in soybean milk
    • Ono T., Takeda M., and Guo S.T. Interaction of protein particles with lipids in soybean milk. Bioscience Biotechnology & Biochemistry 60 7 (1996) 1165-1169
    • (1996) Bioscience Biotechnology & Biochemistry , vol.60 , Issue.7 , pp. 1165-1169
    • Ono, T.1    Takeda, M.2    Guo, S.T.3
  • 19
    • 4444265418 scopus 로고    scopus 로고
    • Emulsifying properties and surface behavior of native and denatured whey soy proteins in comparison with other proteins. Creaming stability of oil-in-water emulsions
    • Palazolo G.G., Sorgentini D.A., and Wagner J.R. Emulsifying properties and surface behavior of native and denatured whey soy proteins in comparison with other proteins. Creaming stability of oil-in-water emulsions. Journal of the American Oil Chemists' Society 81 7 (2004) 625-632
    • (2004) Journal of the American Oil Chemists' Society , vol.81 , Issue.7 , pp. 625-632
    • Palazolo, G.G.1    Sorgentini, D.A.2    Wagner, J.R.3
  • 22
    • 0035186748 scopus 로고    scopus 로고
    • Gel formation by β-conglycinin and glycinin and their mixtures
    • Renkema J.M.S., Knabben J.H.M., and van Vliet T. Gel formation by β-conglycinin and glycinin and their mixtures. Food Hydrocolloids 15 4-6 (2001) 407-414
    • (2001) Food Hydrocolloids , vol.15 , Issue.4-6 , pp. 407-414
    • Renkema, J.M.S.1    Knabben, J.H.M.2    van Vliet, T.3
  • 23
    • 0344788843 scopus 로고
    • Nitrogen solubility index, isolated protein yield, and whey nitrogen content of several soybean strains
    • Smith A.K., Rackis J.J., Isnardi P., Cartter J.L., and Krober O.A. Nitrogen solubility index, isolated protein yield, and whey nitrogen content of several soybean strains. Cereal Chemistry 43 (1966) 261-270
    • (1966) Cereal Chemistry , vol.43 , pp. 261-270
    • Smith, A.K.1    Rackis, J.J.2    Isnardi, P.3    Cartter, J.L.4    Krober, O.A.5
  • 24
    • 0033272010 scopus 로고    scopus 로고
    • Comparative study of structural characteristics and thermal behavior of whey and isolate soybean proteins
    • Sorgentini D.A., and Wagner J.R. Comparative study of structural characteristics and thermal behavior of whey and isolate soybean proteins. Journal of Food Biochemistry 23 5 (1999) 489-507
    • (1999) Journal of Food Biochemistry , vol.23 , Issue.5 , pp. 489-507
    • Sorgentini, D.A.1    Wagner, J.R.2
  • 25
  • 26
    • 85170004090 scopus 로고    scopus 로고
    • The thermo-stability analysis of whey soybean protein (WSP) and the interaction between WSP and soybean globulin
    • (in Chinese, with English abstract)
    • Tie X.Y., and Guo S.T. The thermo-stability analysis of whey soybean protein (WSP) and the interaction between WSP and soybean globulin. Science and Technology of Food Industry 27 9 (2006) 77-80 (in Chinese, with English abstract)
    • (2006) Science and Technology of Food Industry , vol.27 , Issue.9 , pp. 77-80
    • Tie, X.Y.1    Guo, S.T.2
  • 27
    • 33845471438 scopus 로고
    • Heat-induced interactions between soybean proteins: preferential association of 11S basic subunits and β subunits of 7S
    • Utsumi S., Damodaran S., and Kinsella J.E. Heat-induced interactions between soybean proteins: preferential association of 11S basic subunits and β subunits of 7S. Journal of Agricultural and Food Chemistry 32 6 (1984) 1406-1412
    • (1984) Journal of Agricultural and Food Chemistry , vol.32 , Issue.6 , pp. 1406-1412
    • Utsumi, S.1    Damodaran, S.2    Kinsella, J.E.3
  • 28
    • 0037070503 scopus 로고    scopus 로고
    • Structure-function relationships of soybean proteins revealed by using recombinant systems
    • Utsumi S., Maruyama N., Satoh R., and Adachi M. Structure-function relationships of soybean proteins revealed by using recombinant systems. Enzyme and Microbial Technology 30 (2002) 284-288
    • (2002) Enzyme and Microbial Technology , vol.30 , pp. 284-288
    • Utsumi, S.1    Maruyama, N.2    Satoh, R.3    Adachi, M.4
  • 29
    • 54249125183 scopus 로고    scopus 로고
    • Role of the C-terminal region of β-amylase from barley and additivity of mutational effects of intragenic amino acid replacements on the thermostability of β-amylase
    • Yoshigi N., Okada Y., Maeba H., Sahara H., and Tamaki T. Role of the C-terminal region of β-amylase from barley and additivity of mutational effects of intragenic amino acid replacements on the thermostability of β-amylase. Journal of Applied Glycoscience 43 2 (1996) 227-235
    • (1996) Journal of Applied Glycoscience , vol.43 , Issue.2 , pp. 227-235
    • Yoshigi, N.1    Okada, Y.2    Maeba, H.3    Sahara, H.4    Tamaki, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.