Ohshiro T, Izumi Y
Department of Biotechnology, Tottori University, Japan.
Bioseparation. 2000;9(3):185-8. doi: 10.1023/a:1008181730720.
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.
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。