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乌贼墨多酚氧化酶的部分特性
引用本文:江津津,戚晓玉,周培根.乌贼墨多酚氧化酶的部分特性[J].上海水产大学学报,2002,11(4):353-356.
作者姓名:江津津  戚晓玉  周培根
作者单位:上海水产大学食品学院,上海水产大学食品学院,上海水产大学食品学院 上海 200090,上海 200090,上海 200090
摘    要:以乌贼墨为材料,用0.05mol/L pH7.2的磷酸盐缓冲液提取多酚氧化酶(PPO),30%-80%的硫酸铵分级沉淀后通过DEAE-Sepherose CL-6B层析柱分离,合并具有较高酶活性的洗脱液,透析、浓缩后用于酶的特性研究。通过金属离子对该酶活性影响的研究表明,在mmol/L水平,铜离子和铅离子对该酶具有强烈抑制作用,但铜离子在20μmol/L浓度时,对酶却有显著激活作用。在mmol/L水平,Na^ 、K^ 、Mg^2 和Ca^2 对PPO活性无显著影响。在无机阴离子中HSO3^-对酶活性有强烈抑制作用,在10mmol/L时抑制效率达100%,而Cl^-、Br^-、I^-和SO4^2-则对PPO活性无显著影响。

关 键 词:多酚氧化酶  PPO  乌贼墨  酶学特性  金属离子  无机阴离子  酶活性
文章编号:1004-7271(2002)04-0353-04
修稿时间:2002年9月13日

Some properties of polyphenol oxidase from cuttlefish (Sepia esculenta Hoyle) ink
JIANG Jin-jin,QI Xiao-yu,ZHOU Pei-gen.Some properties of polyphenol oxidase from cuttlefish (Sepia esculenta Hoyle) ink[J].Journal of Shanghai Fisheries University,2002,11(4):353-356.
Authors:JIANG Jin-jin  QI Xiao-yu  ZHOU Pei-gen
Abstract:Polyphenol oxidase(PPO) was extracted from cuttlefish ink with 0.05mol/L pH 7.2 sodium phosphate extraction buffer. The crude extract was fractionated with solid ammonium sulfate of 30% - 80% saturation. After dialysis and concentration, The enzyme solution was purified by DEAE-Sepharose CL-6B column chromatography and a 12.2 fold purification of PPO was obtained. Cu2+ and Pb2+ at level of mmol/L inhibited PPO activity while Na+ , K+ , Mg2+ and Ca2+ have little effect on PPO activity, however PPO was apparently activated by Cu2+ at 20umol/L. PPO activity was strongly inhibited by HSO3 ~ and the activity was completely inhibited at 10mmol/L. Cl- , Br~ , I- and SO42- have almost no effect on PPO activity.
Keywords:polyphenol oxidase(PPO)  cuttlefish ink  enzymatic browning
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