文献类型：期刊文献

英文题名：Temperature-dependent gelation of oyster protein: Structural insights and network formation mechanisms

作者：Liu, Yu[1,2];Tan, Mingtang[1,2,3,4];Chen, Zhongqin[1,2,3,4];Zheng, Huina[1,2,3,4];Gao, Jialong[1,2,3,4];Lin, Haisheng[1,2,3,4];Zhu, Guoping[1,2,3,4];Cao, Wenhong[1,2,3,4]

机构：[1]Guangdong Ocean Univ, Coll Food Sci & Technol, 1 Haida Rd, Zhanjiang 524088, Peoples R China;[2]Natl Res & Dev Branch Ctr Shellfish Proc Zhanjiang, Zhanjiang 524088, Peoples R China;[3]Guangdong Prov Engn Technol Res Ctr Seafood, Zhanjiang 524088, Peoples R China;[4]Guangdong Prov Key Lab Aquat Prod Proc & Safety, Zhanjiang 524088, Peoples R China

年份：2026

卷号：171

外文期刊名：FOOD HYDROCOLLOIDS

收录：SCI-EXPANDED(收录号：WOS:001564922500001)、、WOS

基金：The authors (Yu Liu, Mingtang Tan, Zhongqin Chen, Huina Zheng, Jialong Gao, Haisheng Lin, Guoping Zhu, Wenhong Cao) declare that there are no financial interests or personal relationships that will in-fluence the work reported in this paper. The financial supports for this study by the National Key R & D Pro-gram of China (2024YFD2401902) , the Program of China Agriculture Research System (CARS-49) , and the Shellfish & Algae Industry Inno-vation Team of Guangdong Modern Agricultural Technology System (2024CXTD23) are gratefully acknowledged.

语种：英文

外文关键词：Oyster protein; Gel properties; Protein aggregation; Intermolecular interactions; Microstructure

外文摘要：Oyster (Crassostrea hongkongensis) protein (OP) is a high-quality aquatic protein, and understanding its heat-induced gel formation mechanism is crucial for fully utilizing its potential. This study systematically investigated the effects of different heating temperatures (70-90 degrees C) on the gel properties of OP by examining changes in aggregation behavior, conformational transitions, intermolecular interactions, water distribution, and microstructure. The results demonstrated that OP aggregation increased continuously with temperature, as evidenced by increased particle size and turbidity, accompanied by decreased solubility and absolute zeta potential. Atomic force microscopy (AFM) revealed that moderate heating promoted orderly linear aggregate formation. Higher temperatures induced conformational changes, with beta-sheet content peaking at 80 degrees C alongside a significant decrease in fluorescence intensity. Furthermore, the macroscopic gel properties (water holding capacity, gel strength, and textural properties) exhibited temperature-dependent variations, with the optimum performance observed at 80 degrees C, while excessive heating led to gel deterioration. Analysis of intermolecular interactions and microstructure demonstrated that appropriate heating promoted molecular aggregation by regulating intermolecular interactions, thereby establishing an ideal three-dimensional network that enhanced gel quality. These findings provide novel insights into heat-induced OP gelation and guide the development of high-quality oyster protein-based gel products.