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.
Article
in Chinese
| 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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Chemical Precipitation
/
Soil Microbiology
/
Bacillus
/
Bacterial Proteins
/
Enzyme Stability
/
Chemistry
/
Sarcosine Oxidase
/
Metabolism
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2010
Type:
Article
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