UNDERSTANDING THE STABILIZING PROPERTY OF CASEIN IN HEATED MILK PROTEIN EMULSIONS

摘要

Caseins and whey proteins exist together in bovine milk in the approximate proportions of 80:20. Both kinds of protein are widely valued as food ingredients due to their excellent emulsifying abilities. Yet the different molecular structures give the two types of protein quite distinct functionalities. The globular whey proteins, especially β-lactoglobulin (β-lg), are heat-sensitive proteins and are known to denature above 70 °C. The disordered caseins, on the other hand, are much more stable to heat. As such, their predominance in milk over the whey proteins means that many milk products can withstand quite severe processing treatments at high temperatures without much change in their physico-chemical properties.