Purification and Properties of Hydrogen Sulfide Oxidase from Bacillus sp.BN53-1

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概要

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• A hydrogen sulfide oxidase was purified to homogeneity from the heterotroph Bacillus sp. BN53-1 isolated from pig feces compost. The enzyme was found to be a monomer with a M_r value of approximately 37kDa. It required FAD for its activity, which was not replaced by FMN. The optimum reaction pH and temperature were 7.5 and 40°C, respectively. The enzyme was stable between pH 6.0 and 7.0 and up to 30°C. Its activity was simulated by Ca^<2+> and Mn^<2+> and inhibited by Al^<3+> dithiothreitol, and 2-mercaptoethanol. The main product was elemental sulfur, and H_2O_2 was not detected. The N-terminal sequence of the enzyme showed similarity to other FAD-requiring enzymes.

• 公益社団法人日本生物工学会の論文
• 1999-04-25

著者

• Ohta Yoshiyuki

  Faculty Of Applied Biological Science Hiroshima University

• NAKADA YUJI

  Faculty of Applied Biological Science, Hiroshima University

• Nakada Y

  Ajinomoto Oil Mills Co. Inc. Kanagawa Jpn

• NAKADA Yuji

  Faculty of Agriculture, Tokyo University of Agriculture and Technology

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