9IS0

Ultra-high temperature sterilization-treated beta-conglycinin

9IS0 の概要

• エントリーDOI: 10.2210/pdb9is0/pdb
• 分子名称: Beta-conglycinin beta subunit 2 (1 entity in total)
• 機能のキーワード: beta-conglycinin beta homotrimers, ultra-high temperature sterilization-treated, plant protein
• 由来する生物種: Glycine max (Soybean, Glycine hispida)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 133474.63

構造登録者

Zhang, T.,Li, J.Y. (登録日: 2024-07-16, 公開日: 2025-07-23, 最終更新日: 2026-02-04)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.23 Å)