Whey protein isolate (WPI) was modified by a ternary system containing horseradish peroxidase, glucose oxidase and d-glucose through the one- and two-step protocols, yielding two respective crosslinked products MWPI-1 and MWPI-2 with the enhanced relative dityrosine contents (127.4 and 101.0). Compared with WPI, both MWPI-1 and MWPI-2 had much ordered secondary structure, increased disulfide-bond contents, average particle sizes, surface hydrophobicity, oil-binding capacity, emulsification and thermal stability, but reduced free sulfhydryl groups contents and in vitro digestibility. Moreover, both MWPI-1 and MWPI-2 in dispersions showed higher apparent viscosity, larger viscoelastic moduli than WPI, together with the lower gelling temperatures (67.1 °C and 70.1 °C versus 73.6 °C). Overall, MWPI-1 with a higher crosslinking extent consistently exhibited more remarkable property alteration. It is concluded that the ternary system is an effective approach when aiming to modify secondary structure especially these properties of WPI, such as aggregation, emulsification, gelation, rheology and thermal stability.

乳清蛋白分离物 (WPI) 通过包含辣根过氧化物酶、葡萄糖氧化酶和d-葡萄糖的三元系统通过一步和两步方案进行修饰，产生两种各自的交联产物 MWPI-1 和 MWPI-2，其相对二酪氨酸含量有所提高（127.4 和 101.0）。与WPI相比，MWPI-1和MWPI-2均具有更有序的二级结构，增加了二硫键含量、平均粒径、表面疏水性、油结合能力、乳化性和热稳定性，但降低了游离巯基含量和体外消化率。此外，分散体中的 MWPI-1 和 MWPI-2 均表现出比 WPI 更高的表观粘度、更大的粘弹性模量，以及更低的胶凝温度（67.1 °C 和 70.1 °C与73.6°C）。总体而言，具有更高交联度的 MWPI-1 始终表现出更显着的性能改变。结论是三元体系是一种有效的方法，旨在改变二级结构，尤其是 WPI 的这些性质，如聚集、乳化、凝胶、流变和热稳定性。