桑尺蠖多酚氧化酶的纯化及其部分生物化学性质  

Purification and Partial Biochemical Characterization of Polyphenol Oxidase from Phthonandria atrineata(Butler)

作　　者：张永亮[1,2] 曾媛琴[3] 贾永红[4] 柳照应[1] 艾均文[1] 朱勇[1] 

机构地区：[1]西南大学生物技术学院 [2]周口师范学院生命科学系,河南周口466001 [3]西南大学生命科学学院 [4]廊坊师范学院生命科学系

出　　处：《西南大学学报（自然科学版）》2007年第9期86-90,共5页Journal of Southwest University(Natural Science Edition)

基　　金：教育部博士学科点专项基金(20060635008);重庆市教委基金资助项目(040208)

摘　　要：经硫酸铵分级沉淀,Sephadex G-100凝胶过滤等步骤,使桑尺蠖Phthonandria atrineata(Butler)多酚氧化酶纯化,纯化倍数为6.28倍.该酶对焦性没食子酸、邻苯二酚和L-多巴的Km值分别为9.64 mmol/L、6.82 mmol/L和4.30 mmol/L.这种多酚氧化酶在pH=7.0,37℃时活性最高.利用多种氧化酶抑制剂对该酶活性的抑制结果表明,所用抑制剂对其均有不同程度的抑制作用.此外,该酶对EDTA和金属离子比较敏感.The kinetic properties of polyphenol oxidase （PPO） in Phthonandria atrineata （Butler） were studied after the enzyme was partially purified by saturated （NH4）2SO4 and Sephadex G-100 gel filtration. The results showed that a 6.28-fold purification was achieved from the crude enzyme. The affinities of PPO with the substrates pyrogallol, catechol and L-dopamine （L-DOPA） were different, the Km with the three substrates being 9. 64, 6.82 and 4.30mmol/L, respectively. The optimum pH was 7.0 and the best temperature was 37℃ for the tested PPO. All the inhibitors studied showed, in different degrees, inhibitory effects on PPO activity. In addition, this enzyme proved to be comparatively sensitive to EDTA and metal ions.

关 键 词：桑尺蠖 多酚氧化酶 纯化 抑制剂 性质 

分 类 号：S433.4[农业科学—农业昆虫与害虫防治] Q55[农业科学—植物保护]