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Volumn 163, Issue , 2014, Pages 114-119

Structure and property modification of an oligochitosan-glycosylated and crosslinked soybean protein generated by microbial transglutaminase

Author keywords

Crosslinking; Functional property; Glycosylation; Oligochitosan; Soybean protein; Structure; Transglutaminase

Indexed keywords

CROSSLINKING; DICHROISM; ELECTROPHORESIS; EMULSIFICATION; GLYCOSYLATION; INFRARED SPECTROSCOPY; MOLAR RATIO; SOYBEAN OIL; STRUCTURE (COMPOSITION);

EID: 84901271451     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2014.04.089     Document Type: Article
Times cited : (104)

References (41)
  • 1
    • 23744480550 scopus 로고    scopus 로고
    • Functional and thermal properties of wheat, barley, and soy flours and their blends treated with a microbial transglutaminase
    • H.J. Ahn, J.H. Kim, and P.K.W. Ng Functional and thermal properties of wheat, barley, and soy flours and their blends treated with a microbial transglutaminase Journal of Food Science 70 2005 380 386
    • (2005) Journal of Food Science , vol.70 , pp. 380-386
    • Ahn, H.J.1    Kim, J.H.2    Ng, P.K.W.3
  • 2
    • 84901255111 scopus 로고    scopus 로고
    • Changes in functional properties by transglutaminase cross linking as a function of pH of legumes protein isolate
    • N.A. Ali, S.H. Ahmed, E.A. Mohamed, I.A.M. Ahmed, and E.E. Babiker Changes in functional properties by transglutaminase cross linking as a function of pH of legumes protein isolate Innovative Romanian Food Biotechnology 7 2010 12 20
    • (2010) Innovative Romanian Food Biotechnology , vol.7 , pp. 12-20
    • Ali, N.A.1    Ahmed, S.H.2    Mohamed, E.A.3    Ahmed, I.A.M.4    Babiker, E.E.5
  • 3
    • 0028022532 scopus 로고
    • Quantitative determination of monosaccharides in glycoproteins by high-performance liquid chromatography with highly sensitive fluorescence detection
    • DOI 10.1006/abio.1994.1338
    • K.R. Anumula Quantitative determination of monosaccharides in glycoproteins by high-performance liquid chromatography with highly sensitive fluorescence detection Analytical Biochemistry 220 1994 275 283 (Pubitemid 24261169)
    • (1994) Analytical Biochemistry , vol.220 , Issue.2 , pp. 275-283
    • Anumula, K.R.1
  • 4
    • 0019005874 scopus 로고
    • Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism
    • S. Brahms, and J. Brahms Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism Journal of Molecular Biology 138 1980 149 178
    • (1980) Journal of Molecular Biology , vol.138 , pp. 149-178
    • Brahms, S.1    Brahms, J.2
  • 7
    • 85022241054 scopus 로고
    • Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk protein
    • F.C. Church, H.E. Swaisgood, D.H. Porter, and G.L. Catignani Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk protein Journal of Dairy Science 66 1983 1219 1227
    • (1983) Journal of Dairy Science , vol.66 , pp. 1219-1227
    • Church, F.C.1    Swaisgood, H.E.2    Porter, D.H.3    Catignani, G.L.4
  • 8
    • 0036813333 scopus 로고    scopus 로고
    • Transglutaminase catalyzed reactions: Impact on food applications
    • G.A.H. de Jong, and S.J. Koppelman Transglutaminase catalyzed reactions: Impact on food applications Journal of Food Science 67 2002 2798 2806 (Pubitemid 35376151)
    • (2002) Journal of Food Science , vol.67 , Issue.8 , pp. 2798-2806
    • De Jong, G.A.H.1    Koppelman, S.J.2
  • 9
    • 19944398453 scopus 로고    scopus 로고
    • Rheological properties and stability of model salad dressing emulsions prepared with a dry-heated soybean protein isolate-dextran mixture
    • DOI 10.1016/j.foodhyd.2005.01.003, PII S0268005X05000287
    • N.G. Diftis, C.G. Biliaderis, and V.D. Kiosseoglou Rheological properties and stability of model salad dressing emulsions prepared with a dry-heated soybean protein isolate-dextran mixture Food Hydrocolloids 19 2005 1025 1031 (Pubitemid 40759209)
    • (2005) Food Hydrocolloids , vol.19 , Issue.6 , pp. 1025-1031
    • Diftis, N.G.1    Biliaderis, C.G.2    Kiosseoglou, V.D.3
  • 10
    • 0038693085 scopus 로고    scopus 로고
    • Improvement of emulsifying properties of soybean protein isolate by conjugation with carboxymethyl cellulose
    • DOI 10.1016/S0308-8146(02)00236-4, PII S0308814602002364
    • N.G. Diftis, and V. Kiosseoglou Improvement of emulsifying properties of soybean protein isolate by conjugation with carboxymethyl cellulose Food Chemistry 81 2003 1 6 (Pubitemid 36801973)
    • (2003) Food Chemistry , vol.81 , Issue.1 , pp. 1-6
    • Diftis, N.1    Kiosseoglou, V.2
  • 11
    • 0242349227 scopus 로고    scopus 로고
    • High-performance liquid chromatographic determination of neutraceuticals, glucosamine sulphate and chitosan, in raw materials and dosage forms
    • DOI 10.1016/S0003-2670(02)00279-9, PII S0003267002002799
    • Y.S. El-Saharty, and A.A. Bary High-performance liquid chromatographic determination of neutraceuticals, glucosamine sulphate and chitosan, in raw materials and dosage forms Analytica Chimica Acta 462 2002 125 131 (Pubitemid 37337959)
    • (2002) Analytica Chimica Acta , vol.462 , Issue.1 , pp. 125-131
    • El-Saharty, Y.S.1    Bary, A.A.2
  • 12
    • 0002856011 scopus 로고
    • Chemical modification of proteins: An overview
    • R.E. Feeney, J.R. Whitaker, American Chemical Society Washington, D.C
    • R.E. Feeney, R.B. Yamasaki, and K.F. Geoghegan Chemical modification of proteins: An overview R.E. Feeney, J.R. Whitaker, Modification of proteins 1982 American Chemical Society Washington, D.C 1 54
    • (1982) Modification of Proteins , pp. 1-54
    • Feeney, R.E.1    Yamasaki, R.B.2    Geoghegan, K.F.3
  • 13
    • 33749653542 scopus 로고    scopus 로고
    • Conjugation of sodium caseinate and gum arabic catalyzed by transglutaminase
    • DOI 10.1021/jf061220k
    • J. Flanagan, and H. Singh Conjugation of sodium caseinate and gum arabic catalyzed by transglutaminase Journal of Agricultural and Food Chemistry 54 2006 7305 7310 (Pubitemid 44554956)
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , Issue.19 , pp. 7305-7310
    • Flanagan, J.1    Singh, H.2
  • 14
    • 31844444482 scopus 로고    scopus 로고
    • Microwave improvement of soy protein isolate-saccharide graft reactions
    • J.J. Guan, A.Y. Qiu, X.Y. Liu, Y.F. Hua, and Y.H. Ma Microwave improvement of soy protein isolate-saccharide graft reactions Food Chemistry 97 2006 577 585
    • (2006) Food Chemistry , vol.97 , pp. 577-585
    • Guan, J.J.1    Qiu, A.Y.2    Liu, X.Y.3    Hua, Y.F.4    Ma, Y.H.5
  • 15
    • 84985200365 scopus 로고
    • Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins
    • S. Hayakawa, and S. Nakai Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins Journal of Food Science 50 1985 486 491
    • (1985) Journal of Food Science , vol.50 , pp. 486-491
    • Hayakawa, S.1    Nakai, S.2
  • 16
    • 40849133923 scopus 로고    scopus 로고
    • The effects of transglutaminase on the functional properties of the myofibrillar protein concentrate obtained from beef heart
    • A. Ionescu, I. Aprodu, A. Darabǎ, and L. Pornealǎ The effects of transglutaminase on the functional properties of the myofibrillar protein concentrate obtained from beef heart Meat Science 79 2008 278284
    • (2008) Meat Science , vol.79 , pp. 278284
    • Ionescu, A.1    Aprodu, I.2    Darabǎ, A.3    Pornealǎ, L.4
  • 17
    • 77955762508 scopus 로고    scopus 로고
    • Transglutaminase-induced cross-linking and glucosamine conjugation in soybean protein isolates and its impacts on some functional properties of the products
    • S.J. Jiang, and X.H. Zhao Transglutaminase-induced cross-linking and glucosamine conjugation in soybean protein isolates and its impacts on some functional properties of the products European Food Research and Technology 231 2010 679 689
    • (2010) European Food Research and Technology , vol.231 , pp. 679-689
    • Jiang, S.J.1    Zhao, X.H.2
  • 18
    • 79951514973 scopus 로고    scopus 로고
    • Transglutaminase-induced cross-linking and glucosamine conjugation of casein and some functional properties of the modified product
    • S.J. Jiang, and X.H. Zhao Transglutaminase-induced cross-linking and glucosamine conjugation of casein and some functional properties of the modified product International Dairy Journal 21 2011 198 205
    • (2011) International Dairy Journal , vol.21 , pp. 198-205
    • Jiang, S.J.1    Zhao, X.H.2
  • 19
    • 84866403945 scopus 로고    scopus 로고
    • Cross-linking and glucosamine conjugation of casein by transglutaminase and the emulsifying property and digestibility in vitro of the modified product
    • S.J. Jiang, and X.H. Zhao Cross-linking and glucosamine conjugation of casein by transglutaminase and the emulsifying property and digestibility in vitro of the modified product International Journal of Food Properties 15 2012 1286 1299
    • (2012) International Journal of Food Properties , vol.15 , pp. 1286-1299
    • Jiang, S.J.1    Zhao, X.H.2
  • 20
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins
    • A. Kato, and S. Nakai Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins Biochimica et Biophysica Acta 624 1980 13 20
    • (1980) Biochimica et Biophysica Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 21
    • 36849156983 scopus 로고
    • Sensitivity of circular dichroism to protein tertiary structure class
    • P. Manavalan, and W.C. Johnson Sensitivity of circular dichroism to protein tertiary structure class Nature 305 1983 831 832
    • (1983) Nature , vol.305 , pp. 831-832
    • Manavalan, P.1    Johnson, W.C.2
  • 22
    • 0034633083 scopus 로고    scopus 로고
    • A review of Maillard reaction in food and implications to kinetic modelling
    • DOI 10.1016/S0924-2244(01)00022-X, PII S092422440100022X
    • S.I. Martins, W.M. Jongen, and M.A. van Boekel A review of Maillard reaction in food and implications to kinetic modelling Trends in Food Science & Technology 11 2000 364 373 (Pubitemid 32516039)
    • (2000) Trends in Food Science and Technology , vol.11 , Issue.9-10 , pp. 364-373
    • Martins, S.I.F.S.1    Jongen, W.M.F.2    Van Boekel, M.A.J.S.3
  • 23
    • 60249095273 scopus 로고    scopus 로고
    • Importance of size and charge of carbohydrate chains in the preparation of functional glycoproteins with excellent emulsifying properties from tofu whey
    • A.O. Matemu, H. Kayahara, H. Murasawa, and S. Nakamura Importance of size and charge of carbohydrate chains in the preparation of functional glycoproteins with excellent emulsifying properties from tofu whey Food Chemistry 114 2009 13281334
    • (2009) Food Chemistry , vol.114 , pp. 13281334
    • Matemu, A.O.1    Kayahara, H.2    Murasawa, H.3    Nakamura, S.4
  • 26
    • 84907421510 scopus 로고
    • The relationship between the method of preparation and the structural and functional properties of soy protein isolates. Part I: Structural and hydration properties
    • S. Petruccelli, and M.C. Añón The relationship between the method of preparation and the structural and functional properties of soy protein isolates. Part I: Structural and hydration properties Journal of Agricultural and Food Chemistry 42 1994 2161 2169
    • (1994) Journal of Agricultural and Food Chemistry , vol.42 , pp. 2161-2169
    • Petruccelli, S.1    Añón, M.C.2
  • 27
    • 0031423685 scopus 로고    scopus 로고
    • Solubility and emulsifying properties of soy protein isolates modified by pancreatin
    • M. Qi, N.S. Hettiarachchy, and U. Kalapathy Solubility and emulsifying properties of soy protein isolates modified by pancreatin Journal of Food Science 62 1997 1110 1115 (Pubitemid 28106989)
    • (1997) Journal of Food Science , vol.62 , Issue.6 , pp. 1110-1115
    • Qi, M.1    Hettiarachchy, N.S.2    Kalapathy, U.3
  • 28
    • 0002787444 scopus 로고
    • Functionality of soy proteins
    • N.S. Hettiararchy, G.R. Ziegler, Marcel Dekker New York
    • K.C. Rhee Functionality of soy proteins N.S. Hettiararchy, G.R. Ziegler, Protein functionality in food systems 1994 Marcel Dekker New York 311 324
    • (1994) Protein Functionality in Food Systems , pp. 311-324
    • Rhee, K.C.1
  • 30
    • 68349148846 scopus 로고    scopus 로고
    • Physicochemical properties of three food proteins treated with transglutaminase
    • L.H.B. Soares, P.M. Albuquerque, F. Assmann, and M.A.Z. Ayub Physicochemical properties of three food proteins treated with transglutaminase Ciência Rural 34 2004 1219 1223
    • (2004) Ciência Rural , vol.34 , pp. 1219-1223
    • Soares, L.H.B.1    Albuquerque, P.M.2    Assmann, F.3    Ayub, M.A.Z.4
  • 31
    • 84886278621 scopus 로고    scopus 로고
    • Rheological, gelling and emulsifying properties of a glycosylated and cross-linked caseinate generated by transglutaminase
    • C.L. Song, and X.H. Zhao Rheological, gelling and emulsifying properties of a glycosylated and cross-linked caseinate generated by transglutaminase International Journal of Food Science & Technology 48 2013 2595 2602
    • (2013) International Journal of Food Science & Technology , vol.48 , pp. 2595-2602
    • Song, C.L.1    Zhao, X.H.2
  • 32
    • 84892435740 scopus 로고    scopus 로고
    • The preparation of an oligochitosan-glycosylated and cross-linked caseinate obtained by a microbial transglutaminase and its functional properties
    • C.L. Song, and X.H. Zhao The preparation of an oligochitosan-glycosylated and cross-linked caseinate obtained by a microbial transglutaminase and its functional properties International Journal of Dairy Technology 67 2014 110 116
    • (2014) International Journal of Dairy Technology , vol.67 , pp. 110-116
    • Song, C.L.1    Zhao, X.H.2
  • 33
    • 4143054391 scopus 로고    scopus 로고
    • Chemistry of the casein
    • P.F. Fox, P.L.H. McSweeney, Kluwer Academic/Plenum Publishers New York
    • H.E. Swaisgood Chemistry of the casein P.F. Fox, P.L.H. McSweeney, Advanced dairy chemistry-1. Proteins 2003 Kluwer Academic/Plenum Publishers New York 155
    • (2003) Advanced Dairy chemistry-1. Proteins , pp. 155
    • Swaisgood, H.E.1
  • 34
    • 27544441069 scopus 로고    scopus 로고
    • Effect of transglutaminase treatment on the properties of cast films of soy protein isolates
    • DOI 10.1016/j.jbiotec.2005.06.020, PII S0168165605003305
    • C.H. Tang, Y. Jiang, Q.B. Wen, and X.Q. Yang Effect of transglutaminase treatment on the properties of cast films of soy protein isolates Journal of Biotechnology 120 2005 296 307 (Pubitemid 41540386)
    • (2005) Journal of Biotechnology , vol.120 , Issue.3 , pp. 296-307
    • Tang, C.-H.1    Jiang, Y.2    Wen, Q.-B.3    Yang, X.-Q.4
  • 35
    • 55649086169 scopus 로고    scopus 로고
    • Transglutaminase-induced cross-linking of vicilin-rich kidney protein isolate: Influence on the functional properties and in vitro digestibility
    • C.H. Tang, X. Sun, S.W. Yin, and C.Y. Ma Transglutaminase-induced cross-linking of vicilin-rich kidney protein isolate: Influence on the functional properties and in vitro digestibility Food Research International 41 2008 941 947
    • (2008) Food Research International , vol.41 , pp. 941-947
    • Tang, C.H.1    Sun, X.2    Yin, S.W.3    Ma, C.Y.4
  • 36
    • 0000557371 scopus 로고    scopus 로고
    • Structure-function relationships of soy proteins
    • S. Damodaran, A. Paraf, Marcel Dekker New York
    • S. Utsumi, Y. Matsumura, and T. Mori Structure-function relationships of soy proteins S. Damodaran, A. Paraf, Food proteins and their applications 1997 Marcel Dekker New York 259 264
    • (1997) Food Proteins and Their Applications , pp. 259-264
    • Utsumi, S.1    Matsumura, Y.2    Mori, T.3
  • 37
    • 23644445987 scopus 로고    scopus 로고
    • Glucosylation of β-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics
    • DOI 10.1110/ps.051405005
    • A.M. van Teeffelen, K. Broersen, and H.H. de Jongh Glucosylation of β-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics Protein Science 14 2005 2187 2194 (Pubitemid 41132383)
    • (2005) Protein Science , vol.14 , Issue.8 , pp. 2187-2194
    • Van Teeffelen, A.M.M.1    Broersen, K.2    De Jongh, H.H.J.3
  • 38
    • 33750430615 scopus 로고    scopus 로고
    • Gelation behavior of wheat gluten by heat treatment followed by transglutaminase cross-linking reaction
    • J.S. Wang, M.M. Zhao, X.Q. Yang, Y.M. Jiang, and C. Chun Gelation behavior of wheat gluten by heat treatment followed by transglutaminase cross-linking reaction Food Hydrocolloids 21 2007 174179
    • (2007) Food Hydrocolloids , vol.21 , pp. 174179
    • Wang, J.S.1    Zhao, M.M.2    Yang, X.Q.3    Jiang, Y.M.4    Chun, C.5
  • 39
    • 33749608762 scopus 로고    scopus 로고
    • β-Lactoglobulin-dextran Maillard conjugates: Their effect on interfacial thickness and emulsion stability
    • DOI 10.1016/j.jcis.2006.07.081, PII S0021979706007004
    • T.J. Wooster, and M.A. Augustin β-Lactoglobulin-dextran Maillard conjugates: Their effect on interfacial thickness and emulsion stability Journal of Colloid and Interface Science 303 2006 564 572 (Pubitemid 44547955)
    • (2006) Journal of Colloid and Interface Science , vol.303 , Issue.2 , pp. 564-572
    • Wooster, T.J.1    Augustin, M.A.2
  • 41
    • 84863267579 scopus 로고    scopus 로고
    • Improvement of emulsifying properties of Maillard reaction products from β-conglycinin and dextran using controlled enzymatic hydrolysis
    • J.B. Zhang, N.N. Wu, X.Q. Yang, X.T. He, and L.J. Wang Improvement of emulsifying properties of Maillard reaction products from β-conglycinin and dextran using controlled enzymatic hydrolysis Food Hydrocolloids 28 2012 301 312
    • (2012) Food Hydrocolloids , vol.28 , pp. 301-312
    • Zhang, J.B.1    Wu, N.N.2    Yang, X.Q.3    He, X.T.4    Wang, L.J.5


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