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Purificiation and Some Properties of Polyphenol Oxidase from Van Apple(Golden Delicious)

机译:范苹果(金冠)多酚氧化酶的纯化及部分性质

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Polyphenol oxidase was isolated from van apple,with a 4.0-fold purification of polyphenol oxidase by ammonium sulfate and DEAE cellulose being achieved.The optimum pH was 4 and for this enzyme,the optimum temperature was 50deg C.V_(max)and K_m values were found of Lineweaver-Burk graphs.Potassium cyanide,benzoic acid,citric acid,MnCl_2,NaCl,NaNO_2 and CuSO_4 were used as inhibitors.The enzyme activity was inhibited by benzoic acid,CuSO_4 and NaCl,polyphenol oxidase activity at 10 mM,whereas NaNO_2,citric acid,KCN and MnCl_2 enhanced by polyphenol oxidase activity at 10 mM.
机译:从范苹果中分离出多酚氧化酶,用硫酸铵和DEAE纤维素对多酚氧化酶进行了4.0倍纯化。最适pH为4,最适温度为50℃。V_(max)和K_m值分别用氰化钾,苯甲酸,柠檬酸,MnCl_2,NaCl,NaNO_2和CuSO_4作抑制剂。苯甲酸,CuSO_4和NaCl对酶的活性有抑制作用,而多酚氧化酶的活性在10 mM时受到抑制。 NaNO_2,柠檬酸,KCN和MnCl_2在10 mM时被多酚氧化酶活性增强。

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