References

• Ahn, H. J., Kim, J. H., & Ng, P. K. W. (2005). Functional and thermal properties of wheat, barley, and soy flours and their blends treated with a microbial transglutaminase. Journal of Food Science, 70, c380–c386. doi:10.1111/j.1365-2621.2005.tb11433.x
   Web of Science ®Google Scholar
• AOAC. (1995). Official methods of analysis (16th ed.). Arlington, VA: Association of Official Analytical Chemists.
   Google Scholar
• Batista, M. K. S., Pinto, L. F., Gomes, C. A. R., & Gomes, P. (2006). Novel highly-soluble peptide-chitosan polymers: Chemical synthesis and spectral characterization. Carbohydrate Polymers, 64, 299–305. doi:10.1016/j.carbpol.2005.11.040
   Web of Science ®Google Scholar
• Beuchat, L. R. (1977). Functional and electrophoretic characteristics of succinylated peanut flour protein. Journal of Agricultural and Food Chemistry, 25, 258–261. doi:10.1021/jf60210a044
   Web of Science ®Google Scholar
• Church, F. C., Swaisgood, H. E., Porter, D. H., & Catignani, G. L. (1983). Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. Journal of Dairy Science, 66, 1219–1227. doi:10.3168/jds.S0022-0302(83)81926-2
   Web of Science ®Google Scholar
• Diftis, N., & Kiosseoglou, V. (2006). Physicochemical properties of dry-heated soy protein isolate–dextran mixtures. Food Chemistry, 96, 228–233. doi:10.1016/j.foodchem.2005.02.036
   Web of Science ®Google Scholar
• E1-Saharty, Y. S., & Bary, A. A. (2002). High-performance liquid chromatographic determination of neutraceuticals, glucosamine sulphate and chitosan, in raw materials and dosage forms. Analytica Chimica Acta, 462, 125–131. doi:10.1016/S0003-2670(02)00279-9
   Web of Science ®Google Scholar
• Gauche, C., Vieira, J. T. C., Ogliari, P. J., & Bordignon-Luiz, M. T. (2008). Crosslinking of milk whey proteins by transglutaminase. Process Biochemistry, 43, 788–794. doi:10.1016/j.procbio.2008.04.004
   Web of Science ®Google Scholar
• Guan, Y., Tian, Y., Li, Y., Yang, Z. F., Jia, Y. Y., Hang, T. J., & Wen, A. D. (2011). Application of a liquid chromatographic/tandem mass spectrometric method to a kinetic study of derivative glucosamine in healthy human urine. Journal of Pharmaceutical and Biomedical Analysis, 55, 181–186. doi:10.1016/j.jpba.2011.01.012
   PubMed Web of Science ®Google Scholar
• Hassan, A. B., Osman, G. A., & Babiker, E. E. (2007). Effect of chymotrypsin digestion followed by polysaccharide conjugation or transglutaminase treatment on functional properties of millet proteins. Food Chemistry, 102, 257–262. doi:10.1016/j.foodchem.2006.04.043
   Web of Science ®Google Scholar
• Hayakawa, S., & Nakai, S. (1985). Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. Journal of Food Science, 50, 486–491. doi:10.1111/j.1365-2621.1985.tb13433.x
   Web of Science ®Google Scholar
• Hermansson, A. M. (1986). Soy protein gelation. Journal of the American Oil Chemists Society, 63, 658–666. doi:10.1007/BF02638232
   Web of Science ®Google Scholar
• Hiller, B., & Lorenzen, P. C. (2008). Surface hydrophobicity of physicochemically and enzymatically treated milk proteins in relation to techno-functional properties. Journal of Agricultural and Food Chemistry, 56, 461–468. doi:10.1021/jf072400c
   PubMed Web of Science ®Google Scholar
• Huppertz, T., Fox, P. F., De Kruif, K. G., & Kelly, A. L. (2006). High pressure-induced changes in bovine milk proteins: A review. Biochimica Et Biophysica Acta (Bba)-Proteins and Proteomics, 1764, 593–598. doi:10.1016/j.bbapap.2005.11.010
   PubMed Web of Science ®Google Scholar
• Jiang, S.-J., & Zhao, X.-H. (2010). 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, 679–689. doi:10.1007/s00217-010-1319-2
   Web of Science ®Google Scholar
• Jiang, S.-J., & Zhao, X.-H. (2011). Transglutaminase-induced cross-linking and glucosamine conjugation of casein and some functional properties of the modified product. International Dairy Journal, 21, 198–205. doi:10.1016/j.idairyj.2010.12.004
   Web of Science ®Google Scholar
• Kato, A., Mifuru, R., Matsudomi, N., & Kobayashi, K. (1992). Functional casein- polysaccharide conjugates prepared by controlled dry heating. Bioscience, Biotechnology and Biochemistry, 56, 567–571. doi:10.1271/bbb.56.567
   PubMed Web of Science ®Google Scholar
• Kim, S. K. (2011). Chitin, chitosan, oligosaccharides and their derivatives. Boca Raton, FL: CRC Press.
   Google Scholar
• Li, C. P., Enomoto, H., Ohki, S., Ohtomo, H., & Aoki, T. (2005). Improvement of functional properties of whey protein isolate through glycation and phosphorylation by dry heating. Journal of Dairy Science, 88, 4137–4145. doi:10.3168/jds.S0022-0302(05)73099-X
   PubMed Web of Science ®Google Scholar
• Liu, M., & Damodaran, S. (1999). Effect of transglutaminase-catalyzed polymerization of β-casein on its emulsifying properties. Journal of Agricultural and Food Chemistry, 47, 1514–1519. doi:10.1021/jf981030c
   PubMed Web of Science ®Google Scholar
• Liu, Y., Zhao, G. L., Zhao, M. M., Ren, J. Y., & Yang, B. (2012). Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction. Food Chemistry, 131, 901–906. doi:10.1016/j.foodchem.2011.09.074
   Web of Science ®Google Scholar
• Marciniak-Darmochwal, K., & Kostyra, H. (2009). Influence of nonenzymatic glycosylation (glycation) of pea proteins (Pisum sativum) on their susceptibility to enzymatic hydrolysis. Journal of Food Biochemistry, 33, 506–521. doi:10.1111/jfbc.2009.33.issue-4
   Web of Science ®Google Scholar
• Martins, S. I., Jongen, W. M., & Van Boekel, M. A. (2000). A review of Maillard reaction in food and implications to kinetic modelling. Trends in Food Science and Technology, 11, 364–373. doi:10.1016/S0924-2244(01)00022-X
   Web of Science ®Google Scholar
• Matemu, A. O., Kayahara, H., Murasawa, H., & Nakamura, S. (2009). Importance of size and charge of carbohydrate chains in the preparation of functional glycoproteins with excellent emulsifying properties from tofu whey. Food Chemistry, 114, 1328–1334. doi:10.1016/j.foodchem.2008.11.011
   Web of Science ®Google Scholar
• Mizuno, A., Mitsuiki, M., Motoki, M., Ebisawa, K., & Suzuki, E. (2000). Relationship between the glass transition of soy protein and molecular structure. Journal of Agricultural and Food Chemistry, 48, 3292–3297. doi:10.1021/jf991151s
   PubMed Web of Science ®Google Scholar
• Motoki, M., Nio, N., & Takinami, K. (1984). Functional properties of food proteins polymerized by transglutaminase. Agricultural and Biological Chemistry, 48, 1257–1261. doi:10.1271/bbb1961.48.1257
   Web of Science ®Google Scholar
• Muzzarelli, R. A. A., Boudrant, J., Meyer, D., Manno, N., DeMarchis, M., & Paoletti, M. G. (2012). Current views on fungal chitin/chitosan, human chitinases, food preservation, glucans, pectins and inulin: A tribute to Henri Braconnot, precursor of the carbohydrate polymers science, on the chitin bicentennial. Carbohydrate Polymers, 87, 995–1012. doi:10.1016/j.carbpol.2011.09.063
   Web of Science ®Google Scholar
• Oliver, C. M., Melton, L. D., & Stanley, R. A. (2006). Creating proteins with novel functionality via the Maillard reaction: A review. Critical Reviews in Food Science and Nutrition, 46, 337–350. doi:10.1080/10408690590957250
   PubMed Web of Science ®Google Scholar
• Petruccelli, S., & Anon, M. C. (1994). Relationship between the method of obtention and the structural and functional properties of soy proteins isolates. 1. Structural and hydration properties. Journal of Agricultural and Food Chemistry, 42, 2161–2169. doi:10.1021/jf00046a017
   Web of Science ®Google Scholar
• Roos, N., Lorenzen, P. C., Sick, H., Schrezenmeir, J., & Schlimme, E. (2003). Cross-linking by transglutaminase changes neither the in vitro proteolysis nor the in vivo digestibility of caseinate. Kieler Milchwirtschaftliche Forschungsberichte, 55, 261–276.
   Google Scholar
• Schmid, M., Sängerlaub, S., Wege, L., & Stäbler, A. (2014). Properties of transglutaminase crosslinked whey protein isolate coatings and cast films. Packaging Technology and Science, 27, 799–817. doi:10.1002/pts.v27.10
   Web of Science ®Google Scholar
• Seguro, K., Kumazawa, Y., Kuraishi, C., Sakamoto, H., & Motoki, M. (1996). The epsilon-(gamma-glutamyl) lysine moiety in crosslinked casein is an available source of lysine for rats. The Journal of Nutrition, 126, 2557–2562.
   PubMed Web of Science ®Google Scholar
• Silverstein, P. M., Webster, F. X., & Kiemle, D. J. (2005). Spectrometric identification of organic compounds. Hoboken, NJ: John Wiley & Sons Press.
   Google Scholar
• Song, C.-L., & Zhao, X.-H. (2014). Structure and property modification of an oligochitosan-glycosylated and crosslinked soybean protein generated by microbial transglutaminase. Food Chemistry, 163, 114–119. doi:10.1016/j.foodchem.2014.04.089
   PubMed Web of Science ®Google Scholar
• Tang, C.-H., Jiang, Y., Wen, Q.-B., & Yang, X.-Q. (2005). Effect of transglutaminase treatment on the properties of cast films of soy protein isolates. Journal of Biotechnology, 120, 296–307. doi:10.1016/j.jbiotec.2005.06.020
   PubMed Web of Science ®Google Scholar
• Tang, C.-H., Wu, H., Chen, Z., & Yang, X.-Q. (2006). Formation and properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase. Food Research International, 39, 87–97. doi:10.1016/j.foodres.2005.06.004
   Web of Science ®Google Scholar
• Tian, M., Chen, F., Ren, D. W., Yu, X. X., Zhang, X. H., Zhong, R., & Wan, C. X. (2010). Preparation of a series of chitooligomers and their effect on hepatocytes. Carbohydrate Polymers, 79, 137–144. doi:10.1016/j.carbpol.2009.07.039
   Web of Science ®Google Scholar
• Xue, F., Li, C., Zhu, X. W., Wang, L. F., & Pan, S. Y. (2013). Comparative studies on the physicochemical properties of soy protein isolate-maltodextrin and soy protein isolate-gum acacia conjugate prepared through Maillard reaction. Food Research International, 51, 490–495. doi:10.1016/j.foodres.2013.01.012
   Web of Science ®Google Scholar
• Zhang, Q. B., Ames, J. M., Smith, R. D., Baynes, J. W., & Metz, T. O. (2009). A perspective on the Maillard reaction and the analysis of protein glycation by mass spectrometry: Probing the pathogenesis of chronic disease. Journal of Proteome Research, 8, 754–769. doi:10.1021/pr800858h
   PubMed Web of Science ®Google Scholar
• Zhu, C.-Y., Wang, X.-P., & Zhao, X.-H. (2015). Property modification of caseinate responsible to transglutaminase-induced glycosylation and crosslinking in the presence of a degraded chitosan. Food Science and Biotechnology, 24, 843–850. doi:10.1007/s10068-015-0109-9
   Web of Science ®Google Scholar