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Structure and property modification of an oligochitosan-glycosylated and crosslinked soybean protein generated by microbial transglutaminase
- Song, Chun-Li, Zhao, Xin-Huai
- Food chemistry 2014 v.163 pp. 114-119
- binding capacity, chitosan, circular dichroism spectroscopy, crosslinking, droplets, electrophoresis, emulsifying properties, emulsions, glucosamine, glycosylation, hydrophobicity, infrared spectroscopy, oils, pH, protein content, protein-glutamine gamma-glutamyltransferase, soy protein
- The impacts of oligochitosan glycosylation and crosslinking on the structure and properties of a soybean protein were investigated. The reaction was carried out by transglutaminase with 10kUkg−1 protein at pH 7.5 and 37°C for 3h, under a protein content of 40gl−1 and a molar ratio of acyl donor to oligochitosan acceptor of 1:3. The modified protein contained glucosamine at a concentration of 12.1gkg−1 protein. Electrophoresis and infrared spectroscopy analysis confirmed the modified protein to be crosslinked and glycosylated. Circular dichroism analysis showed the modified protein possessed a decreased α-helix and β-structure. The modified protein exhibited lower surface hydrophobicity and emulsifying activity but higher emulsion stability than the soybean protein, it also had better water and oil binding capacity (12.2g and 3.5mlg−1 protein, respectively), and could form a thicker protein outer layer in the oil droplets in emulsion. Transglutaminase-induced oligochitosan glycosylation and crosslinking is thus able to modify soybean proteins.