Extraction, partial purification and characterization of polyphenol oxidase from tea leaf (Camellia sinensis).
Müge Ünal, S. N. Yabacı, Aysun Şener
Abstract
Müge Ünal, S. N. Yabacı, Aysun Şener
Abstract
Polyphenol oxidase (PPO) from tea leaves was extracted and partially purified through (NH 4)2SO 4 precipitation, dialysis and ion exchange chromatography. Of the substrates tested, 4-methylcatechol was the best substrate for PPO with a K m value of 127.8 mM. The optimum pH for PPO activity was found to be 6.02. The enzyme showed high activity over a broad pH range of 4.03-7.00. The optimum temperature for PPO activity was 30 °C. The enzyme had more than 70% of the maximum activity between 20-80 °C. Energy of activation (Ea) and Z values were found to be 58.301 kJ/mol ( r 2 = 0.961) and 39.68°C ( r 2 = 0.965), respectively. Of the inhibitors
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Polyphenol oxidase (PPO) from tea leaves was extracted and partially purified through (NH 4)2SO 4 precipitation, dialysis and ion exchange chromatography. Of the substrates tested, 4-methylcatechol was the best substrate for PPO with a K m value of 127.8 mM. The optimum pH for PPO activity was found to be 6.02. The enzyme showed high activity over a broad pH range of 4.03-7.00. The optimum temperature for PPO activity was 30 °C. The enzyme had more than 70% of the maximum activity between 20-80 °C. Energy of activation (Ea) and Z values were found to be 58.301 kJ/mol ( r 2 = 0.961) and 39.68°C ( r 2 = 0.965), respectively. Of the inhibitors
Key concepts: Polyphenol oxidase, Camellia sinensis, Chemistry, Catechol oxidase, Substrate (aquarium), Extraction (chemistry), Polyphenol, Enzyme