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Volumn 42, Issue 10, 2009, Pages 1373-1380

Gelling of microbial transglutaminase cross-linked soy protein in the presence of ribose and sucrose

Author keywords

Cross linking; Maillard reaction; Microbial transglutaminase; Ribose; Soy protein isolate gels

Indexed keywords

FLOW BEHAVIOURS; INCUBATION PERIODS; MAILLARD; MAILLARD REACTION; MICROBIAL TRANSGLUTAMINASE; MICROBIAL TRANSGLUTAMINASE (MTGASE); PARTICLE SHAPE; PROTEIN ANALYSIS; PROTEIN FRACTIONS; PROTEIN NETWORK; REDUCING SUGARS; RHEOLOGICAL STUDIES; RIBOSE; SDS-PAGE; SOY PROTEIN; SOY PROTEIN ISOLATE GELS; SOY PROTEIN ISOLATES; SUGAR SOLUTIONS;

EID: 70349769186     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2009.07.001     Document Type: Article
Times cited : (25)

References (40)
  • 2
    • 84985269010 scopus 로고
    • Maillard browning of common amino acids and sugars
    • Ashoor S.H., and Zent J.B. Maillard browning of common amino acids and sugars. Journal of Food Science 49 (1984) 1206-1207
    • (1984) Journal of Food Science , vol.49 , pp. 1206-1207
    • Ashoor, S.H.1    Zent, J.B.2
  • 3
    • 33846610642 scopus 로고    scopus 로고
    • Improvement of dough rheology, bread quality and bread shelf-life by enzymes combination
    • Caballero P.A., Gómez M., and Rosell C.M. Improvement of dough rheology, bread quality and bread shelf-life by enzymes combination. Journal of Food Engineering 81 (2007) 42-53
    • (2007) Journal of Food Engineering , vol.81 , pp. 42-53
    • Caballero, P.A.1    Gómez, M.2    Rosell, C.M.3
  • 5
    • 0030094209 scopus 로고    scopus 로고
    • Network formation and viscoelastic properties of commercial soy protein dispersions: Effect of heat treatment, pH and calcium ions
    • Chronakis I.S. Network formation and viscoelastic properties of commercial soy protein dispersions: Effect of heat treatment, pH and calcium ions. Food Research International 29 (1996) 123-134
    • (1996) Food Research International , vol.29 , pp. 123-134
    • Chronakis, I.S.1
  • 6
    • 0002016231 scopus 로고
    • Gels and gelling
    • Schwartzberg H.G., and Hartel R.W. (Eds), Marcel Dekker Inc, New York
    • Clark A.H. Gels and gelling. In: Schwartzberg H.G., and Hartel R.W. (Eds). Physical chemistry of foods (1992), Marcel Dekker Inc, New York 263-305
    • (1992) Physical chemistry of foods , pp. 263-305
    • Clark, A.H.1
  • 7
    • 0000536558 scopus 로고
    • Gelation of globular proteins
    • Mitchell J.R., and Ledward D.A. (Eds), Elsevier Applied Science Publisher Ltd
    • Clark A.H., and Lee-Tuffnell C.D. Gelation of globular proteins. In: Mitchell J.R., and Ledward D.A. (Eds). Functional properties of food macromolecules (1986), Elsevier Applied Science Publisher Ltd 203-272
    • (1986) Functional properties of food macromolecules , pp. 203-272
    • Clark, A.H.1    Lee-Tuffnell, C.D.2
  • 8
    • 33845279681 scopus 로고
    • Refolding of thermally unfolded soy proteins during the cooling regime of the gelation process: Effect on gelation
    • Damodaran S. Refolding of thermally unfolded soy proteins during the cooling regime of the gelation process: Effect on gelation. Journal of Agricultural and Food Chemistry 36 (1988) 262-269
    • (1988) Journal of Agricultural and Food Chemistry , vol.36 , pp. 262-269
    • Damodaran, S.1
  • 9
    • 0001042101 scopus 로고    scopus 로고
    • Amino acids, peptides, and proteins
    • Fennema W.R. (Ed), Marcel Dekker, Inc, New York
    • Damodaran S. Amino acids, peptides, and proteins. In: Fennema W.R. (Ed). Food chemistry (1996), Marcel Dekker, Inc, New York 335-365
    • (1996) Food chemistry , pp. 335-365
    • Damodaran, S.1
  • 11
    • 0000326990 scopus 로고
    • Transglutaminase (Guinea Pig liver)
    • Tabor H., and Tabor W.C. (Eds), Academic Press, New York
    • Folk J.E. Transglutaminase (Guinea Pig liver). In: Tabor H., and Tabor W.C. (Eds). Methods in enzymology (1970), Academic Press, New York 889-894
    • (1970) Methods in enzymology , pp. 889-894
    • Folk, J.E.1
  • 12
    • 46049101599 scopus 로고    scopus 로고
    • Physicochemical properties and microstructures of soy protein isolate gels produced using combined cross-linking treatments of microbial transglutaminase
    • Gan C.Y., Cheng L.H., and Easa A.M. Physicochemical properties and microstructures of soy protein isolate gels produced using combined cross-linking treatments of microbial transglutaminase. Food Research International 41 (2008) 600-605
    • (2008) Food Research International , vol.41 , pp. 600-605
    • Gan, C.Y.1    Cheng, L.H.2    Easa, A.M.3
  • 15
    • 0036877087 scopus 로고    scopus 로고
    • Maillard crosslinking of food proteins I: The reaction of glutaraldehyde, formaldehyde, and glyceraldehyde with ribonuclease
    • Gerrard J.A., Brown P.K., and Fayle S.E. Maillard crosslinking of food proteins I: The reaction of glutaraldehyde, formaldehyde, and glyceraldehyde with ribonuclease. Food Chemistry 79 (2002) 343-349
    • (2002) Food Chemistry , vol.79 , pp. 343-349
    • Gerrard, J.A.1    Brown, P.K.2    Fayle, S.E.3
  • 16
    • 0030582431 scopus 로고    scopus 로고
    • A comprehensive survey of the acid-stable fluorescent cross-links formed by ribose with basic amino acids, and partial characterization of a novel Maillard cross-link
    • Graham L. A comprehensive survey of the acid-stable fluorescent cross-links formed by ribose with basic amino acids, and partial characterization of a novel Maillard cross-link. Biochimica et Biophysica Acta 1297 (1996) 9-16
    • (1996) Biochimica et Biophysica Acta , vol.1297 , pp. 9-16
    • Graham, L.1
  • 18
    • 0001429097 scopus 로고    scopus 로고
    • Linking protein using the Maillard reaction and the implications for food processors
    • O'Brien J., Nursten H.E., Crabbe M.J.C., and Ames J.M. (Eds), The Royal Society of Chemistry, United Kingdom
    • Hill S., and Easa A.M. Linking protein using the Maillard reaction and the implications for food processors. In: O'Brien J., Nursten H.E., Crabbe M.J.C., and Ames J.M. (Eds). The Maillard reaction in foods and medicine (1998), The Royal Society of Chemistry, United Kingdom 133-138
    • (1998) The Maillard reaction in foods and medicine , pp. 133-138
    • Hill, S.1    Easa, A.M.2
  • 19
    • 33645726443 scopus 로고    scopus 로고
    • Transglutaminase in dairy products: Chemistry, physics, applications
    • Jaros D., Partschefeld C., Henle T., and Rohm H. Transglutaminase in dairy products: Chemistry, physics, applications. Journal of Texture Studies 37 (2006) 113-155
    • (2006) Journal of Texture Studies , vol.37 , pp. 113-155
    • Jaros, D.1    Partschefeld, C.2    Henle, T.3    Rohm, H.4
  • 20
    • 33748192961 scopus 로고    scopus 로고
    • Skin gelatin from bigeye snapper and brownstripe red snapper: Chemical compositions and effect of microbial transglutaminase on gel properties
    • Jongjareonrak A., Benjakul S., Visessanguan W., and Tanaka M. Skin gelatin from bigeye snapper and brownstripe red snapper: Chemical compositions and effect of microbial transglutaminase on gel properties. Food Hydrocolloids 20 (2006) 1216-1222
    • (2006) Food Hydrocolloids , vol.20 , pp. 1216-1222
    • Jongjareonrak, A.1    Benjakul, S.2    Visessanguan, W.3    Tanaka, M.4
  • 21
    • 0022566930 scopus 로고
    • Effects of temperature food proteins and its implications on functional properties
    • Kilara A., and Sharkasi T.Y. Effects of temperature food proteins and its implications on functional properties. CRC Critical Reviews in Food Science and Nutrition 23 (1985) 323-395
    • (1985) CRC Critical Reviews in Food Science and Nutrition , vol.23 , pp. 323-395
    • Kilara, A.1    Sharkasi, T.Y.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of head bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0038286512 scopus 로고    scopus 로고
    • Gelation of soy glycinin: Influence of pH and ionic strength on network structure in relation to protein conformation
    • Lakemond C.M.M., Jongh H.H.J., Paques M., van Vliet T., Gruppen H., and Voragen A.G.J. Gelation of soy glycinin: Influence of pH and ionic strength on network structure in relation to protein conformation. Food Hydrocolloids 17 (2003) 365-377
    • (2003) Food Hydrocolloids , vol.17 , pp. 365-377
    • Lakemond, C.M.M.1    Jongh, H.H.J.2    Paques, M.3    van Vliet, T.4    Gruppen, H.5    Voragen, A.G.J.6
  • 24
    • 34247580129 scopus 로고    scopus 로고
    • Effects of varying time/temperature-conditions of pre-heating and enzymatic cross-linking on techno-functional properties of reconstituted dairy ingredients
    • Lorenzen P.C. Effects of varying time/temperature-conditions of pre-heating and enzymatic cross-linking on techno-functional properties of reconstituted dairy ingredients. Food Research International 40 (2007) 700-708
    • (2007) Food Research International , vol.40 , pp. 700-708
    • Lorenzen, P.C.1
  • 27
    • 84985180960 scopus 로고
    • Gelation mechanism of soybean 11S globulin: Formation of soluble aggregates as transient intermediates
    • Mori T., Nakamura T., and Utsumi S. Gelation mechanism of soybean 11S globulin: Formation of soluble aggregates as transient intermediates. Journal of Food Science 47 (1981) 26-30
    • (1981) Journal of Food Science , vol.47 , pp. 26-30
    • Mori, T.1    Nakamura, T.2    Utsumi, S.3
  • 28
    • 0001989848 scopus 로고
    • Behaviour of intermediate bond formation in the late stage of heat-induced gelation of glycinin
    • Mori T., Nakamura T., and Utsumi S. Behaviour of intermediate bond formation in the late stage of heat-induced gelation of glycinin. Journal of Agricultural and Food Chemistry 34 (1986) 33-36
    • (1986) Journal of Agricultural and Food Chemistry , vol.34 , pp. 33-36
    • Mori, T.1    Nakamura, T.2    Utsumi, S.3
  • 31
    • 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 (2001) 407-414
    • (2001) Food Hydrocolloids , vol.15 , pp. 407-414
    • Renkema, J.M.S.1    Knabben, J.H.M.2    van Vliet, T.3
  • 32
    • 0002968747 scopus 로고
    • Viscosity of proteins
    • Mitchell J.R., and Ledward D.A. (Eds), Elsevier Applied Science Publisher Ltd
    • Rha C., and Pradipasena P. Viscosity of proteins. In: Mitchell J.R., and Ledward D.A. (Eds). Functional properties of food macromolecules (1986), Elsevier Applied Science Publisher Ltd 79-120
    • (1986) Functional properties of food macromolecules , pp. 79-120
    • Rha, C.1    Pradipasena, P.2
  • 33
    • 84907421527 scopus 로고
    • Effects of thermal treatment of so protein isolate on the characteristics and structure-functional relationship of soluble and insoluble fractions
    • Sorgentini D.A., Wagner J.R., and Añón M.C. Effects of thermal treatment of so protein isolate on the characteristics and structure-functional relationship of soluble and insoluble fractions. Journal of Agricultural and Food Chemistry 43 (1995) 2471-2479
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , pp. 2471-2479
    • Sorgentini, D.A.1    Wagner, J.R.2    Añón, M.C.3
  • 34
    • 34248329577 scopus 로고    scopus 로고
    • Effect of thermal pretreatment of raw soymilk on the gel strength and microstructure of tofu by microbial transglutaminase
    • Tang C.H. Effect of thermal pretreatment of raw soymilk on the gel strength and microstructure of tofu by microbial transglutaminase. LWT-Food Science and Technology 40 (2007) 1403-1409
    • (2007) LWT-Food Science and Technology , vol.40 , pp. 1403-1409
    • Tang, C.H.1
  • 35
    • 33645903211 scopus 로고    scopus 로고
    • Effects of transglutaminase treatment on the thermal properties of soy protein isolates
    • Tang C.H., Chen Z., Li L., and Yang X.Q. Effects of transglutaminase treatment on the thermal properties of soy protein isolates. Food Research International 39 (2006) 704-711
    • (2006) Food Research International , vol.39 , pp. 704-711
    • Tang, C.H.1    Chen, Z.2    Li, L.3    Yang, X.Q.4
  • 36
    • 33846360753 scopus 로고    scopus 로고
    • Formation and rheological properties of 'cold-set' tofu induced by microbial transglutaminase
    • Tang C.H., Li L., Wang J.L., and Yang X.Q. Formation and rheological properties of 'cold-set' tofu induced by microbial transglutaminase. LWT-Food Science and Technology 40 (2007) 579-586
    • (2007) LWT-Food Science and Technology , vol.40 , pp. 579-586
    • Tang, C.H.1    Li, L.2    Wang, J.L.3    Yang, X.Q.4
  • 37
    • 26844437327 scopus 로고    scopus 로고
    • Formation and properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase
    • Tang C.H., Wu H., Chen Z., and Yang X.Q. Formation and properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase. Food Research International 39 (2006) 87-97
    • (2006) Food Research International , vol.39 , pp. 87-97
    • Tang, C.H.1    Wu, H.2    Chen, Z.3    Yang, X.Q.4
  • 38
    • 0001299616 scopus 로고
    • Enzymatic modification of proteins: Effects of transglutaminase cross-linking on some physical properties of β-lactoglobulin
    • Tanimoto S.Y., and Kinsella J.E. Enzymatic modification of proteins: Effects of transglutaminase cross-linking on some physical properties of β-lactoglobulin. Journal of Agricultural and Food Chemistry 36 (1988) 281-285
    • (1988) Journal of Agricultural and Food Chemistry , vol.36 , pp. 281-285
    • Tanimoto, S.Y.1    Kinsella, J.E.2
  • 39
    • 33745190507 scopus 로고    scopus 로고
    • Simultaneous application of transglutaminase and high pressure to improve functional properties of chicken meat gels
    • Trespalacios P., and Pla R. Simultaneous application of transglutaminase and high pressure to improve functional properties of chicken meat gels. Food Chemistry 100 (2007) 264-272
    • (2007) Food Chemistry , vol.100 , pp. 264-272
    • Trespalacios, P.1    Pla, R.2
  • 40
    • 0000810637 scopus 로고
    • Structure function relationship in food proteins: Subunit interactions in heat-induced gelation of 7S, 11S and soy isolate protein
    • Utsumi S., and Kinsella J.E. Structure function relationship in food proteins: Subunit interactions in heat-induced gelation of 7S, 11S and soy isolate protein. Journal of Agricultural and Food Chemistry 33 (1985) 297-303
    • (1985) Journal of Agricultural and Food Chemistry , vol.33 , pp. 297-303
    • Utsumi, S.1    Kinsella, J.E.2


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