title: Heat-induced aggregation and sulphydryl/disulphide reaction products of soy protein with different sulphydryl contents.
abstract: In this study, soy proteins were reduced with 0.1-10mM dithiothreitol (DTT) to obtain an increasing number of sulphydryl groups (SH) with a similar particle size. Aggregation was promoted by increasing the degree of reduction when heated (100°C, 30min), resulting in larger sized aggregates (from 40 to 70nm) and a higher viscosity of the aggregate dispersion. The disulphide bond (SS) content decreased and the less SS linked polymer, which was composed of acidic (A) polypeptide of glycinin, basic (B) polypeptides of glycinin, and a small amount of α' and α subunits of β-conglycinin, was formed with increasing reduction degree, suggesting that SH/SS polymerisation was not the driving force for aggregation. The larger aggregates with increasing degrees of reduction were composed of more B of glycinin and β of β-conglycinin, suggesting that the A and the small amount of α' and α in the SS linked polymer have an inhibiting effect on protein aggregates formation.
authors.affiliation: State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122 Jiangsu Province, PR China; School of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122 Jiangsu Province, PR China.
authors.forename: Qijun
authors.initials: Q
authors.lastname: Ruan
authors.affiliation: State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122 Jiangsu Province, PR China; School of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122 Jiangsu Province, PR China.
authors.forename: Yeming
authors.initials: Y
authors.lastname: Chen
authors.affiliation: State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122 Jiangsu Province, PR China; School of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122 Jiangsu Province, PR China.
authors.forename: Xiangzhen
authors.initials: X
authors.lastname: Kong
authors.affiliation: State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122 Jiangsu Province, PR China; School of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122 Jiangsu Province, PR China. Electronic address: yufeihuajiangnan@126.com.
authors.forename: Yufei
authors.initials: Y
authors.lastname: Hua
mesh_terms: D052179:Antigens, Plant / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry*; D005916:Globulins / Q000737:chemistry*; D006358:Hot Temperature; D010084:Oxidation-Reduction; D010316:Particle Size; D066329:Protein Aggregates; D055314:Seed Storage Proteins / Q000737:chemistry*; D030262:Soybean Proteins / Q000737:chemistry*; D013438:Sulfhydryl Compounds / Q000737:chemistry*; D014783:Viscosity
chemical_list: D052179:Antigens, Plant; D004220:Disulfides; D005916:Globulins; D066329:Protein Aggregates; D055314:Seed Storage Proteins; D030262:Soybean Proteins; D013438:Sulfhydryl Compounds; C013894:beta-conglycinin protein, Glycine max; C011474:glycinin
keywords: Aggregation; Disulphide bond; Heat treatment; Reduction; Sulphydryl