Abstract
The ability of laccase to oxidize polyphenols arouses our interest that laccase can be applied for protein-polyphenol cross-linking. In this study, laccase promoted the cross-linking of gallic acid (GA) and soy protein isolate (SPI) under neutral pH. SPI-GA complexes changed the secondary structures with a decrease in β-fold and an increase in α-helix and β-turn. The free-radical scavenging activity and reducing power determination results suggested that GA elevated the SPI antioxidant activity significantly. Specifically, DPPH free radical scavenging rate and ABTS free radical scavenging ability increased almost 5- and 1.5-fold compared with unmodified SPI, respectively. Moreover, the reducing power had more than 3-fold compared to the SPI control. This study provided a novel enzyme-induced approach to modulate the physicochemical properties of SPI binding polyphenol.
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