机构地区: 安徽师范大学生命科学学院安徽省重要生物资源保护与利用研究省级重点实验室
出 处: 《中国林副特产》 2007年第6期5-7,共3页
摘 要: 研究了败酱多酚氧化酶的酶学性质,结果表明:以邻苯二酚为底物,该酶最适pH为7.8,最适温度为26℃,温度60℃以上酶迅速失活。Vc、NaHSO3、L-Cys能完全抑制酶活性,苯甲酸钠、EDTA等对酶活性有明显的抑制作用。该酶能催化焦性没食子酸、邻苯二酚、愈创木酚氧化,但对焦性没食子酸的亲和力更强。 This paper is an analysis on the kinetic property of polyphenol oxidase (in) patrinia scabiosaefolia Fisch. The result shows that, by using the catechol as the substrate, the most suitable pH value and temperature for this enzyme is at 7.8 and 26℃ respectively, and it will be rapidly inactivated if the temperature gose above 60℃. Vc,NaHSO3, L-Cys can completely inhibit ppo activity; sodium benzonate ang EDTA can remarkably inhibit ppo activity. This enzyme can catalyze the oxidization of catechol and guaiacol, and 1,2,3-hydroxyphenyl, and has higher affinity to 1,2,3-hydroxyphenyl.