豆类蛋白组装机制及其与蛋白加工特性关联性的研究进展

Research Progress on Molecular Assembly Mechanism of Legume Protein and Its Relationship with Protein Processing Properties

摘要:

随着植物基食品消费市场的快速发展,豆类蛋白作为可持续蛋白质资源以及动物蛋白的替代品,在健康食品产业发挥着重要作用。蛋白质组装作为一种有效驱动蛋白质自身及与大分子物质间相互作用的策略在豆类蛋白食品的高效加工中至关重要。概述了pH值、温度、离子、交联酶以及大分子物质等不同条件促使豆类蛋白聚集组装的作用机制以及组装行为与蛋白加工特性之间的关联性。pH值会决定蛋白表面电荷的类型及分布,改变蛋白质的二级结构,促进蛋白质的组装；温度升高不仅使豆类蛋白暴露出某些基团,还可以提高蛋白质扩散和碰撞的速率,加速蛋白质的组装；离子类型及强度分别影响蛋白质周围水的分布及蛋白质间的静电作用,诱导组装行为的发生；交联酶催化豆类蛋白分子内或分子间发生交联,从而驱动豆类蛋白进行聚集组装；多糖和酚类等大分子物质通过与豆类蛋白相互结合,改变蛋白质的结构,为蛋白质的聚集组装提供条件。另外,阐述了豆类蛋白的组装行为对豆类蛋白的加工特性,包括乳化性、发泡性、凝胶性和成膜性的影响,分析了微观变化与加工特性之间的关联性。对豆类蛋白进一步高效利用的发展方向进行了展望,以期为更好地开发高品质的豆类蛋白产品提供理论依据。

Abstract:

With the rapid development of plant-based food consumption market, legume protein, as a sustainable protein resource and a substitute for animal protein, plays an important role in the health food industry. Protein assembly, as an effective strategy to drive protein itself and its interaction with macromolecules, is very important in the efficient processing of legume protein food. The mechanism of aggregation and assembly of legume proteins promoted by pH, temperature, ions, cross-linking enzymes, and macromolecules as well as the relationship between assembly behavior and protein processing properties were summarized. The pH will determine the type and distribution of the surface charge of the protein, change the secondary structure of the protein, and promote the assembly of the protein. The increase in temperature will not only expose some groups of legume protein but also increase the rate of diffusion and collision of the protein, thus accelerating the assembly. The type and strength of ions affect the distribution of water around the protein and the occurrence of assembly induced by electrostatic interaction between proteins. Cross-linking enzymes catalyze intramolecular or intermolecular cross-linking of legume proteins, thus driving legume proteins for aggregation and assembly. Polysaccharides and phenols change the structure of proteins by binding with legume proteins, providing conditions for protein aggregation and assembly. In addition, the effects of assembly behavior of legume proteins on the processing properties of legume proteins, including emulsification, foaming, gel, and film-forming properties were described, and the relationship between microscopic changes and processing properties was analyzed. Finally, the development direction of further efficient utilization of legume protein was prospected, which might provide a theoretical foundation for the better development of high-quality legume protein products.