KMID : 1007520160250000091
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Food Science and Biotechnology 2016 Volume.25 No. 0 p.91 ~ p.96
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Partial Purification and Characterization of Polyphenol Oxidase from Chinese Parsley (Coriandrum sativum)
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Han bin Lin
Allan Wee Ren Ng Chen Wai Wong
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Abstract
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Purification and characterization of polyphenol oxidase (PPO) from Chinese parsley (Coriandrum sativum) were achieved. Crude PPO exhibited an enzyme activity of 1,952.24 EU/mL. PPO was partially purified up to 6.52x with a 10.89% yield using gel filtration chromatography. Maximal PPO activity was found at 35¡ÆC, pH 8.0 for 4-methylcatechol and at 40¡ÆC, pH 7.0 for catechol. PPO showed a higher affinity towards 4-methylcatechol, but a higher thermal stability when reacting with catechol. LCysteine was a better inhibitor than citric acid for reducing PPO activity at concentrations of 1 and 3mM in the presence of either substrate. Two 46 kDa isoenzymes were identified using SDS-PAGE. Isolation and characterization of Chinese parsley serves as a guideline for prediction of enzyme behavior leading to effective prevention of enzymatic browning during processing and storage, including inhibition and inactivation of PPO.
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KEYWORD
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polyphenol oxidase, Chinese parsley, characterization
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