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Characterization of a lactate oxidase from a strain of gram negative bacterium from soil.

Abstract：

:A lactate oxidase was purified about 36-fold from a newly screened strain KY6 of gram negative bacterium from soil to yield a homogeneous protein. The native enzyme had a molecular mass of 204 kDa measured by Sephadex G-200 and that of subunit on the SDS-PAGE was found to be 45 kDa. The enzyme was optimally active at pH 7.7 and showed stability at pH range of 5.7 to 9.5 for 24 h at 4 degrees C. The optimum temperature was 70 degrees C and the enzyme activity was stable for 10 min up to 45 degrees C. The half-life of the enzyme activity was about 10 min at 55 degrees C. The best substrate of the enzyme was D-lactate and Km value for D-lactate was 0.14 mM. The Km value for DL-lactate was 0.20 mM. Substrate inhibition of the enzyme was observed at higher concentrations than 20 mM of DL-lactate and 10 mM of D-lactate.

journal_name

Appl Biochem Biotechnol

journal_title

Applied biochemistry and biotechnology

authors

Xu P,Yano T,Yamamoto K,Suzuki H,Kumagai H

doi

10.1007/BF02786958

subject

Has Abstract

pub_date

1996-03-01 00:00:00

pages

277-88

issue

3

eissn

0273-2289

issn

1559-0291

journal_volume

56

pub_type

杂志文章

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