Abstract: 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.

Key words: glycinin, heat treatment, dissociation-association behavior, gel