Laccase from Streptomyces coelicolor (SLAC) can catalyze protein cross-linking without any phenolic acid assistance, and its effects on the solution and gel properties of whey protein isolate (WPI) were investigated in this study. WPI solution (5% w/v) was catalyzed by SLAC at 60 °C for 10 min at different enzymatic activities (0–20U). Results showed that, cross-linked by SLAC, the foaming capacity and emulsifying activity properties of WPI solution were improved. SLAC treated solutions had more negative charge in zeta potential, indicating more stable in protein solutions. SLAC-modified increased the apparent visicosities of WPI solutions. Rheological results showed that SLAC-treated WPI gels had higher dynamic storage modulus (G′) and took longer gelation time, compared to control (0U). SLAC treatment improved the strength of WPI gels and increased their water holding capacity (WHC). The results indicate that suitable SLAC catalysis could be used to modify whey protein isolate to improve its solution and gel properties.

产链霉菌的漆酶（SLAC）可以催化蛋白质的交联而无需任何酚酸的辅助，并且本研究研究了其对乳清蛋白分离物（WPI）的溶液和凝胶性质的影响。SLAC在60°C下以不同的酶活性（0–20U）催化WPI溶液（5％w / v）。结果表明，通过SLAC交联，WPI溶液的起泡能力和乳化活性得到改善。经SLAC处理的溶液在zeta电位中具有更多的负电荷，表明在蛋白质溶液中更稳定。SLAC修改可增加WPI解决方案的表观粘度。流变学结果表明，与对照（0U）相比，SLAC处理的WPI凝胶具有更高的动态储能模量（G'）和更长的胶凝时间。SLAC处理提高了WPI凝胶的强度，并提高了其保水能力（WHC）。结果表明，合适的SLAC催化可用于修饰乳清蛋白分离物以改善其溶液和凝胶性质。