ArticleFood chemistry: X2022
Hydrophobic bonds-dominated key off-odors/silver carp myofibrillar protein interactions, and their binding characteristics at cold storage and oral temperatures.
Article in Food chemistry: X, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- High-pressure processing mitigates flavor loss in sauced duck legs during storage: Evidence from volatile profiling and myofibrillar protein-flavor compound interactions.Food chemistry: X · 2026Article
- Stearic acid modified nanofiber membranes for flavor improvement of oyster enzymatic hydrolysates: structural characterization and selective adsorption deodorization.Food chemistry: X · 2026Article
- Molecular basis of trypsin's autolysis resistance acetylation for sustained enzymatic activity.Food chemistry: X · 2026Article
- Elucidating Volatile Flavor Profiles and Metabolic Pathways in Northern Pike (Foods (Basel, Switzerland) · 2025Article
- Understanding interactions between four main fishy compounds and grass carp myofibrillar proteins using the SPME-GC-MS, multiple spectroscopy, and molecular docking.Food chemistry: X · 2025Article
- Effects of interactions between microorganisms and lipids on inferior volatile compound production during cold storage of grouper (Food chemistry: X · 2025Article
- Effects of combined binding of chlorogenic acid/caffeic acid and gallic acid to trypsin on their synergistic antioxidant activity, enzyme activity and stability.Food chemistry: X · 2023Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This study revealed the interaction mechanism between silver carp myofibrillar protein (MP) and key off-odors by combining fluorescence spectroscopy with molecular dynamics (MD) simulation. Spectroscopic results exhibited a dynamic quenching mechanism between MP and off-odors. Thermodynamic analysis indicated that the MP/off-odors interaction was spontaneous (ΔG° < 0) and dominated by hydrophobic interactions (ΔH° > 0, ΔS° > 0). Meanwhile, the binding affinity was in the order of nonanal (n = 1.38) > hexanal (n = 0.89) > 1-octen-3-ol (n = 0.65), which was further verified by the MD results. Among off-odors, nonanal had the highest binding energy with myosin (8105.66 kJ/mol) and formed more hydrophobic binding sites to Trp residues in myosin head (e.g., Trp820 and Trp822), thereby changing myosin conformations via both physical and chemical interactions. Additionally, higher binding energies of myosin/off-odors were observed at oral temperature (37 °C) than at cold storage temperature (4 °C), implying that less off-odors were released at 37 °C.
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