Abstract
In order to improve its aqueous solubility and emulsifying function, zein was partially hydrolyzed by trypsin and conjugated to chitosan oligosaccharide lactate by transglutaminase. Hydrolysis and covalent linkage to chitosan oligosaccharide was confirmed by free amine content, gel electrophoresis, and infrared spectroscopy. Enzymatic glycosylation was optimized at pH 6, 44 °C, and 4 h to bind approximately 95% of the free amines in the hydrolysates to chitosan oligosaccharide. Hydrolysis and conjugation increased solubility of zein by 47.60% and 72.93%. Hydrolysis and conjugation also decreased surface hydrophobicity by more than 20% and more than doubled emulsifying activity index, emulsion stability index, and foaming capacity. This enzymatic modification has potential to be applied to improve functional properties of other prolamins.
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