热处理过程中大豆11S球蛋白解离缔合行为研究进展
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摘要
解离缔合反应是大豆蛋白在外界因素影响下蛋白质分子高级结构发生解聚或聚合的过程,是目前植物蛋白领域研究的热点。通常通过热处理使大豆蛋白发生解离缔合反应而改变其构象从而获得理想功能性质;大豆11S球蛋白是大豆蛋白主要成分之一,因此11S球蛋白的热解离缔合行为一定程度上决定了大豆制品的后期加工特性、品质及其应用范围。本文概述了11S球蛋白基本结构的最新研究进展;基于11S球蛋白热处理过程中蛋白浓度差异引起的体系性状变化,综述了离子强度、pH值、大豆7S球蛋白以及大豆脂蛋白对其解离缔合行为的影响;并分析了相应条件下11S球蛋白解离缔合反应机制,以期阐明在热处理过程中11S球蛋白的解离缔合反应机制,为将大豆蛋白解离缔合反应控制在预期范围内,获得高品质的大豆蛋白食品提供理论依据。
The dissociation-association reaction of soybean proteins is the process of depolymerization or polymerization of their higher order structures that is influenced by external factors and is currently a research hotspot of plant proteins.The ideal functional properties of soybean proteins can be obtained by subjecting them to heat treatment, which contributes to conformational changes in soybean proteins by dissociation-association reaction. 11S glycinin is one of the major components of soybean protein. Therefore, the post-processing characteristics, quality and application range of soybean products are determined to a certain extent by the thermal dissociation-association behavior of 11S glycinin. In this paper,the latest progress in the understanding of the fundamental structure of 11S globulin is summarized. Considering that the colloidal properties and dissociation-association behavior of 11S glycinin vary during heating process, depending upon its concentration, the effects of ionic strength, pH, 7S β-conglycinin and soybean lipoprotein on the dissociation-association behavior of 11S glycinin are elucidated, and the underlying mechanism is interpreted. This review hopes to provide theoretical support for controlling the dissociation-association reaction of soybean proteins within the expected range and hence obtaining high-quality soybean protein products.
The dissociation-association reaction of soybean proteins is the process of depolymerization or polymerization of their higher order structures that is influenced by external factors and is currently a research hotspot of plant proteins.The ideal functional properties of soybean proteins can be obtained by subjecting them to heat treatment, which contributes to conformational changes in soybean proteins by dissociation-association reaction. 11S glycinin is one of the major components of soybean protein. Therefore, the post-processing characteristics, quality and application range of soybean products are determined to a certain extent by the thermal dissociation-association behavior of 11S glycinin. In this paper,the latest progress in the understanding of the fundamental structure of 11S globulin is summarized. Considering that the colloidal properties and dissociation-association behavior of 11S glycinin vary during heating process, depending upon its concentration, the effects of ionic strength, pH, 7S β-conglycinin and soybean lipoprotein on the dissociation-association behavior of 11S glycinin are elucidated, and the underlying mechanism is interpreted. This review hopes to provide theoretical support for controlling the dissociation-association reaction of soybean proteins within the expected range and hence obtaining high-quality soybean protein products.
引文
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