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热带假丝酵母HP 15对酚类化合物的降解。II. 降解途径中前两种酶的一些特性。

Degradation of phenolic compounds by the yeast Candida tropicalis HP 15. II. Some properties of the first two enzymes of the degradation pathway.

作者信息

Krug M, Straube G

出版信息

J Basic Microbiol. 1986;26(5):271-81. doi: 10.1002/jobm.3620260505.

Abstract

The first two enzymes of the phenol degradation pathway were determined and characterized in crude extracts from Candida tropicalis HP 15. The phenol hydroxylase (EC 1.14.13.7) was a stable NADPH2- and FAD-dependent enzyme with a pH-optimum of 7.6 to 8.0 and a broad substrate specificity. Influence of ultrasound rapidly reduced the enzyme activity. The catechol 1,2-oxygenase (EC 1.13.1.1) had a broad pH-optimum between 7.5 and 9.6 and a limited substrate specificity. Two active protein bands indicating the presence of two isofunctional enzymes were detectable after electrophoretic separation of crude and partially purified extracts on polyacrylamide gels and specific staining for catechol 1,2-oxygenase activity.

摘要

在热带假丝酵母HP 15的粗提物中测定并表征了苯酚降解途径的前两种酶。苯酚羟化酶(EC 1.14.13.7)是一种稳定的依赖NADPH2和FAD的酶,最适pH为7.6至8.0,底物特异性较广。超声处理会迅速降低该酶的活性。儿茶酚1,2-加氧酶(EC 1.13.1.1)的最适pH范围较宽,在7.5至9.6之间,底物特异性有限。在聚丙烯酰胺凝胶上对粗提物和部分纯化的提取物进行电泳分离,并对儿茶酚1,2-加氧酶活性进行特异性染色后,可检测到两条活性蛋白带,表明存在两种同功酶。

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