Allicin-mediated protection of myofibrillar proteins in refrigerated mandarin fish (Siniperca chuatsi): Molecular interactions with endogenous proteases and inhibition of protein degradation
Year: 2026
Type: article
Abstract: Endogenous proteases accelerate myofibrillar protein (MP) degradation and quality loss in fish. This study investigated allicin's protective effects on refrigerated mandarin fish ( Siniperca chuatsi ). Allicin treatment significantly inhibited cathepsin B, cathepsin L, and calpain activities and reduced MP degradation, leading to lower MFI values and slower accumulation of TCA-soluble peptides. Molecular docking and enzyme assays demonstrated that allicin binds to key catalytic residues of these endogenous proteases, suggesting a multi-target inhibitory mechanism. SDS-PAGE and histological staining further confirmed slower degradation of MPs and collagen, along with improved maintenance of muscle fiber integrity. CD and intrinsic fluorescence confirmed allicin attenuated α-helix loss, delayed tryptophan exposure, and stabilized sulfhydryl groups, indicating protection against oxidative and conformational damage. Overall, allicin inhibits endogenous proteases and preserves protein conformation, highlighting its potential as a natural preservative to improve fish storage quality. • Allicin binds spontaneously to catalytic residues of cathepsin B/L and calpain. • Protease inhibition delays myofibril fragmentation and collagen degradation. • Allicin-treated maintained muscle microstructure integrity and textural properties. • Allicin-mediated protection preserves MP conformation during refrigeration.
Source: Food Chemistry X
Authors: Zhouyi Xiong, Mingqian Zhou, Jihui Wang, Bo Wang, Xuan Chen, Shan Xiao
Language: English
Subfield: Animal Science and Zoology
Domain: Life Sciences
SDG: Zero hunger
Open Access status: gold
Estimated APC paid: $2,330
Award: G4864880464
OpenAlex ID: W7117994373