Purification and characterization of a sarcosine oxidase from Bacillus sp. BSD-8 / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 335-340, 2010.
Artigo
em Chinês
| WPRIM
| ID: wpr-336222
ABSTRACT
We purified a sarcosine oxidase from Bacillus sp. strain BSD-8 isolated from soil. We purified the enzyme by ammonium sulfate precipitation, DEAE-cellulose, Toyopearl hydrophobic and Sephadex G-75 molecular sieve chromatography and characterized the purified sarcosine oxidase. This sarcosine oxidase was a flavin enzyme containing a noncovalently bound flavin with the subunit molecular mass of 51 kDa. The optimal temperature for this enzyme was 60 degrees C and it showed its highest activity at pH 8.5. It was stable in the pH range of 8.0-10.0 and at the temperature of 60 degrees C. Estimated by Lineveaver-Burk plots, the K(m) of the enzyme was 3.1 mmol/L. Ag+, Hg2+, SDS and Tween 80 dramatically inhibted the enzyme activity, whereas Tween 20 and Triton X-100 had no effect on enzyme activity. The thermostability of this enzyme was better than reported sarcosine oxidases, and it could be applied in enzymatic measuring of creatinine.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Precipitação Química
/
Microbiologia do Solo
/
Bacillus
/
Proteínas de Bactérias
/
Estabilidade Enzimática
/
Química
/
Sarcosina Oxidase
/
Metabolismo
Idioma:
Chinês
Revista:
Chinese Journal of Biotechnology
Ano de publicação:
2010
Tipo de documento:
Artigo
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