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 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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