文献类型：期刊文献

英文题名：Identification of Novel Umami Peptides in Douchi and Mechanisms by Sensory Analysis and Molecular Modeling

作者：Liu, Liyan[1,2,3]; Zhao, Huiyan[1]; Jiang, Guili[1]; Xu, Meizhen[1]; Chen, Jianxu[4,5]; Xu, Wenjie[1]; Li, Cuiling[1]; Zhou, Chunxia[1,2,3]; Chen, Jin[1]; Luo, Donghui[1,2,3]

机构：[1] College of Food Science and Technology, College of Food Science and Engineering, Guangdong Ocean University, Zhanjiang, 524088, China; [2] Branch of Chemistry and Chemical Engineering Guangdong Laboratory [Hanjiang Laboratory], Chaozhou, 521000, China; [3] Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, Zhanjiang, 524088, China; [4] Guangdong Mei Wei Yuan Flavours Co., Ltd., Yangjiang, 529500, China; [5] Guangdong Ocean University, China

年份：2025

外文期刊名：SSRN

收录：EI(收录号：20250026797)

语种：英文

外文关键词：High performance liquid chromatography - Hydrogen bonds - Ion chromatography - Ion exchange - Ion exchange resins - Molecular dynamics - Sensory analysis

外文摘要：The study aimed to identify umami peptides from douchi and explore their umami mechanism. Douchi was isolated and purified by ultrafiltration combined with ion-exchange resin and identified by ultra-high performance liquid chromatography-tandem mass spectrometry (UHPLC-MS/MS). Additionally, umami peptides such as TYDGDTEP, VGSEL, FGDEL, IGISIDDH, and RDLL were identified by predictive modeling of umami activity and molecular docking analyses. Sensory evaluation indicated that the umami thresholds for these five umami peptides ranged from 0.5 to 2.0 mg/mL, with TYDGDTEP exhibiting the most potent synergistic umami effect. The molecular docking and simulation results revealed that hydrogen bonding and electrostatic interactions were crucial for forming umami. Besides, the residues Glu148, Lys155, Glu217, Asn150, Asp218, and Asp219 were identified as critical for binding the five umami peptides to the T1R1/T1R3. This study provides the theoretical basis for the processing and application of umami peptides derived from douchi, contributing to understanding these peptides' conformational relationships. ? 2025, The Authors. All rights reserved.