ArticleFood chemistry: X2025
Understanding interactions between four main fishy compounds and grass carp myofibrillar proteins using the SPME-GC-MS, multiple spectroscopy, and molecular docking.
Article in Food chemistry: X, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Regulation of Rainbow Trout Muscle Myofibrillar Networks by Non-Enzymatic Bioactive Compounds fromGels (Basel, Switzerland) · 2026Article
- Competitive Binding of Gingerol Homologs to Fish Myofibrillar Protein Reduces the Retention of Aldehydic Off-Odor Compounds.Foods (Basel, Switzerland) · 2026Article
- Non-covalent interactions between whey protein isolate and taxifolin and their potential application in yogurt.Food chemistry: X · 2026Article
- Formation mechanism and regulation strategies of off-flavors in meat and meat products - An overall perspective.Current research in food science · 2026Review
- Multispectral study on the effects of capsaicin on myofibrillar proteins structure and functional characteristics inFood chemistry: X · 2025Article
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Authors and funding
8 authors.
Funding
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Abstract
The interaction mechanism between four fishy compounds and myofibrillar proteins of grass crap was explored using solid phase microextraction-gas chromatography-mass spectrometry, multispectroscopy, and molecular docking. The result showed that the binding abilities of myofibrillar protein for the fishy compounds decreased in the order of decanal, octanal, hexanal, and 1-octen-3-ol. The interaction between myofibrillar proteins and four fishy compounds affected the aromatic amino acid residue microenvironment. The predominant binding force of myofibrillar proteins to the three aldehydes was hydrophobic, while those to 1-octen-3-ol were hydrogen bonds and van der Waals forces, and binding sites of these compounds occurred near tryptophan and tyrosine. A significant reduction in α-helical content and surface hydrophobicity in grass carp myofibrillar protein upon interaction with the four fishy compounds. Molecular docking confirmed that the different functional groups and chain lengths of the fishy components resulted in different binding sites and binding free energies with grass carp protein.
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