title: Limited aggregation behavior of β-conglycinin and its terminating effect on glycinin aggregation during heating at pH 7.0.
abstract: In this work, different thermal aggregation behaviors of soy β-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 β-conglycinin, forming soluble aggregates. For glycinin, the association between the aggregates that led to the appearance of insoluble materials was observed. Heated with β-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 β-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 β-conglycinin in the solubilization of the soy protein aggregates during heating.
authors.affiliation: Protein Research and Development Center, Department of Food Science and Technology, South China University of Technology, Guangzhou, People's Republic of China.
authors.forename: Jian
authors.initials: J
authors.lastname: Guo
authors.forename: Xiao-Quan
authors.initials: XQ
authors.lastname: Yang
authors.forename: Xiu-Ting
authors.initials: XT
authors.lastname: He
authors.forename: Na-Na
authors.initials: NN
authors.lastname: Wu
authors.forename: Jin-Mei
authors.initials: JM
authors.lastname: Wang
authors.forename: Wei
authors.initials: W
authors.lastname: Gu
authors.forename: Yuan-Yuan
authors.initials: YY
authors.lastname: Zhang
mesh_terms: D052179:Antigens, Plant / Q000737:chemistry*; D002850:Chromatography, Gel; D005916:Globulins / Q000737:chemistry*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D008027:Light; D010316:Particle Size; D017510:Protein Folding; D012542:Scattering, Radiation; D055314:Seed Storage Proteins / Q000737:chemistry*; D012995:Solubility; D030262:Soybean Proteins / Q000737:chemistry*
chemical_list: D052179:Antigens, Plant; D005916:Globulins; D055314:Seed Storage Proteins; D030262:Soybean Proteins; C013894:beta-conglycinin protein, Glycine max; C011474:glycinin