| Autor: |
Öztürk, Cansu, Bayrak, Songül, Demir, Yeliz, Aksoy, Mine, Alım, Zuhal, Özdemir, Hasan, İrfan Küfrevioglu, Ömer |
| Předmět: |
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| Zdroj: |
Biotechnology & Applied Biochemistry; Oct2022, Vol. 69 Issue 5, p2249-2256, 8p |
| Abstrakt: |
Fresh‐cut vegetables and fruits have gained attention among consumers because of their fresh appearance, lack of pollution, nutrition, and convenience. However, in fresh‐cut foods, enzymatic browning is the main problem. Polyphenol oxidase (PPO) is a vital enzyme involved in the process of enzymatic browning. In this study, PPO was purified from potato using Sepharose 4B‐l‐tyrosine‐p‐aminobenzoic acid affinity chromatography and the effect of some indazoles on the enzyme was determined. The enzyme was purified with a specific activity of 52,857.14 EU/mg protein and 21.26‐purification fold. Indazoles exhibited inhibitor properties for PPO with IC50 values in the range of 0.11–1.12 mM and Ki values in the range of 0.15 ± 0.04–3.55 ± 0.88 mM. Among these compounds, 7‐chloro‐1H‐indazole was shown as the most potent PPO inhibitor (Ki: 0.15 ± 0.04 mM). Determination of the enzyme's inhibition kinetics will simplify the testing of candidate PPO inhibitors. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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