Abstract
Whey proteins (WPs) modification can improve their functional properties. To assess the crosslinking characteristics of Bacillus subtilis transglutaminase (BTG), it was used to reacted with WPs (12%, w/v) (40 °C, pH 8.0) for 6 h and 12 h, respectively. Both particle size profile and sodium dodecyl sulfate polyacrylamide gel electrophoresis demonstrated that BTG treatment enhanced the molecular weight of WPs. Meanwhile, BTG crosslinking greatly increased (*P < 0.05) the foaming and emulsifying properties of WPs. Furthermore, the rheological evaluation indicated that the cross-linked WPs showed greater storage modulus and loss modulus in comparison to the native WPs, leading to the increased gel strength. Additionally, BTG-induced WPs gels exhibited significantly enhanced (*P < 0.05) textural properties and water holding capacity. These results suggested the potential of BTG to enhance the functional properties of many proteins in the food industry.
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