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KMID : 0903519960390050349
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1996 Volume.39 No. 5 p.349 ~ p.354
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Purification and Properties of the Polyvinyl alcohol oxidase from Xanthomonas campestris J2Y .
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Abstract
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The Polyvinyl alcohol(PVA) oxidase involved in PVA degradation by microorganism has been purified to homogeneity from culture broth of Xanthomonas campestris J2Y grown in a minimal medium containing PVA as a sole carbon source. The enzyme was purified by DEAE-cellulose chromatograpy and Sephadex G-150 gel filtration. The purified PVA oxidase was electrophoretically homogeneous both in the absence and presence of SDS. The molecular weight of the enzyme was estimated to be about 55,000 daltons by SDS-polyacrylamide gel electrophoresis and Sephadex G-150 gel filtration. The native enzyme existed as a monomer. The optimal pH and temperature was shown to be pH 7 and 37℃ respectively. The activity of enzyme was stable below 55℃ and between pH range of 5∼11. The enzyme activity was significantly inhibited by metal compounds such as Ag^(2+), Hg^(2+). While, metal ions such as Mn^(2+) and Cu^(2+) stimulated the reaction. Km value of the enzyme for PVA was 7.04×10^(-2)mmol/ℓ.
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