PMID: 8984900Mar 1, 1996Paper

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

Applied Biochemistry and Biotechnology
P XuH Kumagai

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.

References

Dec 1, 1967·Journal of Biochemistry·M Tokushige, I W Sizer
Aug 2, 1952·Nature·Y YAMAMURAE KUSUNOSE

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Citations

Jul 15, 2004·Applied Microbiology and Biotechnology·C Q MaY N Zhang
Apr 10, 2008·Journal of Bioscience and Bioengineering·Ping XuCuiqing Ma
May 5, 2007·Prikladnaia biokhimiia i mikrobiologiia·M B KupletskaiaA I Netrusov

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