ArticleFoods (Basel, Switzerland)2023
Comprehensive Multi-Spectroscopy and Molecular Docking Understanding of Interactions between Fermentation-Stinky Compounds and Mandarin Fish Myofibrillar Proteins.
Article in Foods (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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Who cites it
4 citing papers in PubMed.
- Bromelain-induced physicochemical and structural changes in beef myofibrillar proteins and their molecular interaction mechanisms.Food chemistry: X · 2026Article
- Drying-Induced Structural and Oxidative Transformations in Sustainable Proteins: Impact on Physicochemical Properties and Flavor-Binding Functionality.Foods (Basel, Switzerland) · 2026Review
- Gel properties of chicken-squilla low-fat mince gel with inulin: Physicochemical properties, microstructure, intermolecular interactions, and formation mechanism.Food chemistry: X · 2025Article
- Fermented Fish Products: Balancing Tradition and Innovation for Improved Quality.Foods (Basel, Switzerland) · 2024Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The release of flavor compounds is a critical factor that influences the quality of fermented foods. A recent study investigated the interactions between four fermentation-stinky compounds (indole, isovaleric acid, dimethyl disulfide, and dibutyl phthalate) and myofibrillar proteins (MPs). The results indicated that all four fermentation-stinky compounds had different degrees of binding to MPs, with dibutyl phthalate and dimethyl disulfide exhibiting stronger interactions. Reduced hydrophobicity enhanced these interactions. Multi-spectroscopy showed that static fluorescence quenching was dominant in the MPs-fermentation-stinky compound complexes. The interaction altered the secondary structure of MPs, predominantly transitioning from β-sheets to α-helix or random coil structures via hydrogen bond interactions. Molecular docking confirmed that these complexes maintained steady states due to stronger hydrogen bonds, van der Waals forces, ionic bonds, conjugate systems, and lower hydrophobicity interactions. Hence, it is a novel sight that the addition of hydrophobic bond-disrupting agents could improve the flavor of fermented foods.
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Registered trials
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