2011GIDA - Journal of FoodRequires access

Extraction, partial purification and characterization of polyphenol oxidase from tea leaf (Camellia sinensis).

Müge Ünal, S. N. Yabacı, Aysun Şener

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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

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Available 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

Key concepts: Polyphenol oxidase, Camellia sinensis, Chemistry, Catechol oxidase, Substrate (aquarium), Extraction (chemistry), Polyphenol, Enzyme

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Extraction, partial purification and characterization of polyphenol oxidase from tea leaf (Camellia sinensis). — Research Paper | ScholarLens