Purification of Polyphenol Oxidase from Potato and Investigation of the Inhibitory Effects of Phenolic Acids on Enzyme Activity

Bayrak S., Ozturk C., Demir Y., Alim Z., KÜFREVİOĞLU Ö. İ.

PROTEIN AND PEPTIDE LETTERS, sa.3, ss.187-192, 2020 (SCI-Expanded, Scopus) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Basım Tarihi: 2020
  • Doi Numarası: 10.2174/0929866526666191002142301
  • Dergi Adı: PROTEIN AND PEPTIDE LETTERS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, BIOSIS, EMBASE, MEDLINE
  • Sayfa Sayıları: ss.187-192
  • Anahtar Kelimeler: Affinity chromatography, inhibition, phenolic acids, purification, polyphenol oxidase, hydroxybenzoic acid, DERIVATIVES, PLANTS, L.
  • Atatürk Üniversitesi Adresli: Evet

Özet

Background: Polyphenol Oxidase (PPO) belongs to the oxidoreductase enzyme family. Methods: Here, PPO was purified from potato using Sepharose 4B-L-tyrosine-p-aminobenmic 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 K-i 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 (K-i: 0.28 +/- 0.07 mM). Conclusion: Investigating the inhibition kinetics of the enzyme will simplify the testing of PPO inhibitor candidates.