热处理对α-乳白蛋白变性及其与其他乳蛋白相互作用影响的研究进展

Recent Advances in Understanding the Effect of Heat Treatment on α-Lactalbumin Denaturation and Its Interaction with Other Milk Proteins

本文综述了热处理导致的α-乳白蛋白(α-lactalbumin,α-La)变性及其与其他乳蛋白成分之间的相互作用和影响因素。α-La的热稳定性受其分子内结合的Ca2+影响,变性后无法自聚,但可以与β-乳球蛋白(β-lactoglobulin,β-Lg)和血清白蛋白(serum albumin,SA)形成聚集体。经高温短时(high temperature short time,HTST)巴氏杀菌处理生成的α-La/β-Lg聚集体可用于生产低黏度、低浊度和高溶解性的蛋白饮料,α-La/SA聚集体具有良好的凝胶结构。α-La/β-Lg聚集体可与酪蛋白胶束表面的κ-酪蛋白结合,生成的聚合物有利于缩短生产发酵乳的时间,改善酸乳凝胶结构。α-乳白蛋白还能与免疫球蛋白G结合,采用HTST、超巴氏杀菌和超高温灭菌处理可降低乳品的致敏性。在实际生产中可根据需要利用上述反应,选择合适的热处理方式。

In this paper, the effect of heat treatment on the denaturation of α-lactalbumin(α-La) and its interaction with other milk protein components as well as the influencing factors are reviewed. The thermal stability of α-La can be affected by Ca2+ binding. It cannot self-aggregate after denaturation, but can form aggregates with β-lactoglobulin(β-Lg) and serum albumin(SA). Aggregates of α-La/β-Lg produced by high temperature short time(HTST) treatment can be used to produce protein drinks with low viscosity, low turbidity and high solubility. Aggregates of α-La/SA have a good gel structure. α-La/β-Lg aggregates can also combine with κ-casein on the surface of casein micelles, forming polymers that are beneficial to shorten the fermentation process and improve the gel structure of yogurt. The combination of α-La with immunoglobulin G allows reduced allergenicity of milk with HTST, ultra-pasteurization and ultra-high temperature treatments. A suitable heat treatment should be selected in practice to improve the production efficiency.