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Updated: Sep 17, 2025

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
Published on: July 27, 2016
Understanding pyrogallic acid-myofibrillar protein interaction and its effect on flavor release via spectral and
Qiaoyu Liu1, Sili Xiao1, Yun You2
1College of Light Industry and Food Sciences, Academy of Contemporary Agricultural Engineering Innovations, Zhongkai University of Agriculture and Engineering, Guangzhou 510225, China; Guangdong Key Laboratory of Lingnan Specialty Food Science and Technology, Zhongkai University of Agriculture and Engineering, Guangzhou 510225, China; Key Laboratory of Green Processing and Intelligent Manufacturing of Lingnan Specialty Food, Ministry of Agriculture, Guangzhou 510225, China.
Abstract:
The tendency of myofibrillar proteins to adsorb fishy off-flavor impairs processing properties. This study uses natural phenolics to release odors from proteins. The mechanisms underlying the promotion of key fishy off-flavor compounds (KFOCs) released by Pyrogallic acid (PA) through interactions with the myofibrillar protein (MP) of Tilapia were investigated. Fluorescence spectroscopy confirmed the formation of a 1: 1 temperature-sensitive PA-MP complex via static quenching. PA caused significant changes in MP conformation and significantly increased KFOCs release from MP in a dose-effect manner. Molecular docking and molecular dynamics further revealed hydrophobic interactions and hydrogen bonding drove the formation of MP/PA and MP/KFOCs complexes. Binding sites for PA and KFOCs were identified near the Ser129-Glu135 and Asn179-Ser183 residues of myosin. PA exhibited a preferential affinity for myosin binding, thereby influencing the release of KFOCs through competitive interactions.
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