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Inhibition of acid phosphatase, which significantly contributes to inosine 5'-monophosphate (IMP) degradation, is crucial for preventing flavor deterioration of aquatic products during storage. In this study, the inhibitory effect of epicatechin gallate (ECG) on the activity of acid phosphatase isozymes (ACPI and ACPII) was analyzed using inhibition kinetics, fluorescence spectroscopy, isothermal titration calorimetry, and molecular simulation. ACPI and ACPII with molecular weights of 59.5 and 37.3 kDa, respectively, were purified from rainbow trout liver. ECG reversibly inhibited ACPI and ACPII activities via mixed-type inhibition, with half maximal inhibitory concentration (IC 50 ) of 0.24 ± 0.01 mmol/L and 0.27 ± 0.03 mmol/L, respectively. Fluorescence spectra indicated that ECG statically quenched the intrinsic fluorescence of ACPI and ACPII. ECG could spontaneously bind to ACPI and ACPII through hydrogen bonding and van der Waals forces and exhibited a higher affinity for ACPI than for ACPII. In addition, molecular dynamic simulation revealed that ECG-ACPI and ECG-ACPII complexes were relatively stable during the entire simulation process. Our findings provide a theoretical basis for the use of ECG as an inhibitor of ACP to improve the flavor of aquatic products., Competing Interests: Declaration of competing interest There is no conflict of interest., (Copyright © 2024 Elsevier B.V. All rights reserved.)

Trimethylamine-N-oxide demethylase (TMAOase) is a key enzyme for the decomposition of trimethylamine oxide into formaldehyde. The study investigated the inhibitory effects of (+)-catechin on TMAOase and involved mechanism to minimize the formaldehyde (FA) content of seafood during storage. TMAOase was purified by DEAE-52 cellulose and Sephacryl S-300 chromatography and the inhibitory mechanism of TMAOase was studied by Lineweaver-Burk plots, fluorescence spectroscopy, and circular dichroism. Specific activity of 37 ± 0.7 U/mg was obtained with 205 -fold purification and 15% yield, and molecular mass was 25 kDa. (+)-Catechin was a reversible inhibitor of TMAOase and its induced mechanism was the non-competitive inhibition type. (+)-Catechin binding to TMAOase formed a complex with the binding constant (K sv ) of 0.72 × 10 3 at 298 K. The formation of complex induced the static fluorescence quenching and changes in the conformation of TMAOase, leading to a reduction in the rate of catalysis., (Copyright © 2021 Elsevier Ltd. All rights reserved.)