9IS0

Ultra-high temperature sterilization-treated beta-conglycinin

Summary for 9IS0

• Entry DOI: 10.2210/pdb9is0/pdb
• Descriptor: Beta-conglycinin beta subunit 2 (1 entity in total)
• Functional Keywords: beta-conglycinin beta homotrimers, ultra-high temperature sterilization-treated, plant protein
• Biological source: Glycine max (Soybean, Glycine hispida)
• Total number of polymer chains: 3
• Total formula weight: 133474.63

Authors

Zhang, T.,Li, J.Y. (deposition date: 2024-07-16, release date: 2025-07-23, Last modification date: 2026-02-04)

Primary citation

Li, J.,Cai, M.,Liu, Y.,Lv, C.,Zang, J.,Zhao, G.,Zhang, T.
Structural basis for the effects of thermal treatment on soybean seed beta-conglycinin.
Food Res Int, 205:115976-115976, 2025

PubMed Abstract: The production of soy protein in the food industry is inextricably linked to the thermal sterilization process. To gain a deeper understanding of the changes in protein structure during this process, we compared the structural effects of typical thermal sterilization methods (pasteurization and ultra-high temperature sterilization) on β-conglycinin. Chemical characterization of the solutions showed that two thermal sterilization methods did not affect the primary structure and overall morphology of β-conglycinin. However, the α-helix and β-sheet content were reduced. Additionally, the crystal structure of β-conglycinin after different heat treatments was successfully determined by X-ray crystallography. Notably, we precisely observed the sites where the secondary structure was altered at the atomic level. This allowed us to propose a hypothesis that the highly variable continuous antiparallel β-sheet within the C-terminal core β-barrel structural domains may represent an intermediate state influenced by temperature, acting as the initiation site for protein structure dissociation.

PubMed: 40032469
DOI: 10.1016/j.foodres.2025.115976

Experimental method

X-RAY DIFFRACTION (3.23 Å)