Songül Bayrak, Cansu Öztürk, Yeliz Demir*, Zuhal Alım and Ömer İrfan Küfrevioglu Pages 187 - 192 ( 6 )
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 enzyme.
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 inhibitor candidates.
Affinity chromatography, inhibition, phenolic acids, purification, polyphenol oxidase, hydroxybenzoic acid.
Department of Chemistry, Faculty of Sciences, Ataturk University, Erzurum, 25240, Department of Chemistry, Faculty of Sciences, Ataturk University, Erzurum, 25240, Department of Pharmacy Services, Nihat Delibalta Göle Vocational High School, Ardahan University, Ardahan, 75700, Department of Chemistry, Faculty of Science and Arts, Ahievran University, Kırsehir, 40100, Department of Chemistry, Faculty of Sciences, Ataturk University, Erzurum, 25240