文献类型：期刊文献

英文题名：Hot-Air Drying Drives the Formation of Umami Peptides in Oysters by Remodeling the Peptidome and Promoting Interaction with the T1R1/T1R3 Receptor

作者：Cao, Wenhong[1,2,3]; Li, Hui[1]; Yang, Yaofang[1]; Huang, Qianqian[1]; Gao, Jialong[1,2,3]; Tan, Mingtang[1,2,3]; Chen, Zhongqin[1,2,3]; Zheng, Huina[1,2,3]; Lin, Haisheng[1,2,3]

机构：[1] College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, 524088, China; [2] Shenzhen Institute, Guangdong Ocean University, Shenzhen, 518108, China; [3] National Research and Development Branch Center for Shellfish Processing [Zhanjiang], Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Seafood, Zhanjiang, 524088, China

年份：2026

外文期刊名：SSRN

收录：EI(收录号：20260525799)

语种：英文

外文关键词：Binding energy - Bioinformatics - Biosynthesis - Docking - Drying - Electronic assessment - Electronic tongues - Hydrogen bonds - Molecular docking - Molecular modeling - Peptides - Plants (botany) - Sensory perception - Shellfish

外文摘要：Hot-air drying (HAD), a traditional technique in southern China, was investigated for its role in umami enhancement of dried oysters (Crassostrea hongkongensis). Electronic tongue (E-tongue) analysis confirmed a significant increase in umami intensity in dried oyster extracts. Peptidomics identified 1,623 peptides, with GO enrichment revealing preferential thermal degradation of myofibrillar and cytoskeletal proteins. Machine learning prioritized 158 candidate umami peptides. Crucially, HAD selectively enriched medium-chain peptides (8–18 residues) with increased C-terminal Lys/Arg occurrence, a structural signature distinct from conventional umami peptides. Molecular docking showed these features favor robust hydrogen-bonding and electrostatic networks within the T1R1/T1R3 Venus flytrap (VFT) domain (binding energies ? 2026, The Authors. All rights reserved.