KMID : 1134820110400101447
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Journal of the Korean Society of Food Science and Nutrition 2011 Volume.40 No. 10 p.1447 ~ p.1452
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Purification and Characterization of Polyphenol Oxidase from Oyster Mushroom (Pleurotus ostreatus)
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Choi Ju-Hee
Kim Hyeon-Jin Park Sun-Young Ham Kyung-Sik
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Abstract
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Polyphenol oxidase (PPO) isoforms were partially purified from oyster mushroom (Pleurotus ostreatus) using various chromatography techniques, and their characteristics of heat stability, substrate affinity, optimum pH, and optimum temperature were investigated. Three PPO isoforms named PO-¥°, PO-¥±-1, and PO-¥±-2 were partially purified from oyster mushroom. The molecular weight of PO-¥±-1 was 70 kDa and PO-¥° and PO-¥±-2 were less than 6 kDa each. Characterization was carried out using a PPO isoform partially purified by hydrophobic interaction chromatography. Optimum temperature was 55¡É and optimum pH 5.0. However, the PPO was inactivated at neutral pH or by heating at 80¡É for 30 min, while the 40% PPO still remained active after heating at 60¡É for 45 min. The PPO isoform showed the highest substrate affinity to chlorogenic acid and pyrogallol, in which KM values were 1.01 and 2.06 mM, respectively. Therefore, these results suggested that the mushrooms should be stored at a pH higher than 7.0 and at a low temperature to prevent enzymatic browning.
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KEYWORD
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oyster mushroom, polyphenol oxidase, purification, characterization
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