Background: Polyphenol Oxidase (PPO) belongs to the oxidoreductase enzyme family.
Methods: 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
Results: 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).
Conclusion: Investigating the inhibition kinetics of the enzyme will simplify the testing of PPO