Limited Aggregation Behavior of beta-Conglycinin and Its Terminating Effect on Glycinin Aggregation during Heating at pH 7.0

作者：Guo Jian; Yang Xiao Quan^*; He Xiu Ting; Wu Na Na; Wang Jin Mei; Gu Wei; Zhang Yuan Yuan

来源：Journal of Agricultural and Food Chemistry, 2012, 60(14): 3782-3791.

DOI：10.1021/jf300409y

• thermal aggregation
• soy protein
• beta-conglycinin
• glycinin
• soluble aggregates
• insoluble aggregates

In this work, different thermal aggregation behaviors of soy beta-conglycinin and glycinin at pH 7.0 were characterized with size exclusion chromatography and low-angle light scattering. Limited aggregation that grew via the consumption of "monomers" was detected in beta-conglycinin, forming soluble aggregates. For glycinin, the association between the aggregates that led to the appearance of insoluble materials was observed. Heated with beta-conglycinin, the assembly between the glycinin aggregates was terminated and its solubility was recovered. The structure of the soluble and insoluble aggregates was analyzed by small-angle X-ray scattering and dynamic light scattering. Unlike the beta-conglycinin soluble aggregates that possessed limited size and less compact conformation, particles with a denser core and a less dense outer shell were found in the glycinin insoluble aggregates. Evidence is presented to reveal the transition between the soluble and insoluble aggregates and the role of beta-conglycinin in the solubilization of the soy protein aggregates during heating.

• 出版日期2012-4-11
• 单位华南理工大学