Purification of Polyphenol Oxidase from Potato and Investigation of the Inhibitory Effects of Phenolic Acids on Enzyme Activity.
Journal: 2019/October - Protein and Peptide Letters
ISSN: 1875-5305
PUBMED: 31577197
Abstract:Polyphenol oxidase (PPO) belongs to the oxidoreductase enzyme family.Here, PPO was purified from potato using Sepharose 4B-L-tyrosine-p-aminobenzoic acid affinity chromatography. It determined the interactions between some phenolic acids and the enzyme.The enzyme was obtained with a specific activity of 15333.33 EU/mg protein and 7.87-fold purification. It was found that phenolic acids exhibited inhibitory properties for PPO. The IC50 values of the phenolic acids were found in the range of 0.36-2.12 mM, and their Ki values were found in the range of 0.28± 0.07-1.72±0.32 mM. It was determined that studied all studied compounds displayed a competitive inhibition effect. Among these compounds, 3-hydroxybenzoic acid was found to be the most effective PPO inhibitor (Ki: 0.28±0.07 mM).Investigating the inhibition kinetics of the enzyme will simplify the testing of PPO inhibitor candidates.
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