Purification and properties of hydrogen sulfide oxidase from Bacillus sp. BN53-1.
作者： Yuji Nakada , Yoshiyuki Ohta
DOI: 10.1016/S1389-1723(99)80093-0
关键词: Enzyme 、 Sulfur 、 Dithiothreitol 、 Hydrogen sulfide 、 Chemistry 、 Oxidase test 、 Heterotroph 、 Cofactor 、 Biochemistry 、 Bacillales 、 Nuclear chemistry
摘要: A hydrogen sulfide oxidase was purified to homogeneity from the heterotroph Bacillus sp. BN53-1 isolated pig feces compost. The enzyme found be a monomer with Mr value of approximately 37 kDa. It required FAD for its activity, which not replaced by FMN. optimum reaction pH and temperature were 7.5 40°C, respectively. stable between 6.0 7.0 up 30°C. Its activity stimulated Ca2+ Mn2+ inhibited Al3+, dithiothreitol, 2-mercaptoethanol. main product elemental sulfur, H2O2 detected. N-terminal sequence showed similarity other FAD-requiring enzymes.
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