Alcohol hydydrogenase (ADH) is a key enzyme that influences alcohol metabolism in vivo. Our previous study showed that chicken-derived tripeptide KPC could stabilize ADH in a dose-dependant manner. In this study, possible mechanism underlying how KPC could stabilize ADH was further investigated. Fluorescence quenching data showed that KPC induced a dynamic fluorescence quenching with a quenching rate constant value of 1.074 × 1010 M-1s-1, indicating a conformational change. Circular dichroism further suggested a possible transformation from α-helix (14.03%-13.90%) to random coil (31.98-33.04%) in ADH structure as affected by KPC (5mmol/L). Molecular docking analysis predicted that KPC may bind to ADH through hydrophobic interaction and hydrogen bonds. Validation of ADH stabilizing activity of fragment peptides and amino acids from KPC implied the vital role of Cys residue to the bio-activity of KPC. These results indicated that KPC may stabilize ADH through peptide-enzyme interactions, and protect...

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