New Insights into the Inhibition of Hesperetin on Polyphenol Oxidase: Inhibitory Kinetics, Binding Characteristics, Conformational Change and Computational Simulation.

ABSTRACT: The inhibitory activity of hesperetin on polyphenol oxidase (PPO) and their interaction characteristics were investigated using multiple spectroscopic methods and computational simulation. Hesperetin, a mixed inhibitor, reversibly inhibited PPO activity, and its half-maximum inhibitory concentration (IC₅₀) values on monophenolase and diphenolase were 80.8 ± 1.4 μM and 776.0 ± 15.5 μM, respectively. Multivariate curve resolution-alternate least squares (MCR-ALS) analysis suggested PPO interacted with hesperetin and formed PPO-hesperetin complex. Hesperetin statically quenched PPO's endogenous fluorescence, and hydrophobic interactions mainly drove their binding. Hesperetin affected the polarity of the microenvironment around the Trp residues in PPO, but had no effect on that arou

SUBMITTER: Hong X 

PROVIDER: S-EPMC9957399 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature