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用于二苯并噻吩脱硫的酶的纯化、表征及结晶

Purification, characterization and crystallization of enzymes for dibenzothiophene desulfurization.

作者信息

Ohshiro T, Izumi Y

机构信息

Department of Biotechnology, Tottori University, Japan.

出版信息

Bioseparation. 2000;9(3):185-8. doi: 10.1023/a:1008181730720.

Abstract

DszC and DszA, DBT monooxygenase and DBT sulfone monooxygenase, respectively, involved in dibenzothiophene (DBT) desulfurization, were purified to homogeneity from Rhodococcus erythropolis D-1. The two enzymes were crystallized and enzymologically characterized. We found a high activity of flavin reductase in the non-DBT-desulfurizing bacterium, Paenibacillus polymyxa A-1, which is essential for DszC and A activities, and purified to homogeneity and characterized the enzyme.

摘要

分别参与二苯并噻吩(DBT)脱硫的DszC和DszA,即DBT单加氧酶和DBT砜单加氧酶,从红平红球菌D-1中纯化至同质。对这两种酶进行了结晶和酶学表征。我们在非DBT脱硫细菌多粘芽孢杆菌A-1中发现了一种对DszC和A活性至关重要的黄素还原酶的高活性,并将其纯化至同质并对该酶进行了表征。

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