A rapid method for the purification of methanol dehydrogenase from Methylobacterium extorquens |
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Authors: | Liu Qinfeng Kirchhoff Jon R Faehnle Christopher R Viola Ronald E Hudson Richard A |
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Institution: | Department of Chemistry, The University of Toledo, Toledo, OH 43606, USA. |
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Abstract: | Methanol dehydrogenase (MDH) is a water soluble quinoprotein that catalyzes the oxidation of methanol as an important carbon source in methylotrophic bacteria. A rapid method for the purification of MDH from Methylobacterium extorquens AM1 was developed using a single cation exchange chromatographic step, followed by ultrafiltration for final purification, enzyme concentration, and buffer exchange. MDH was obtained in an excellent overall yield with a final enzyme purity of greater than 97%. Storage at -80 degrees C in 20mM phosphate buffer, pH 7.0, showed only a negligible loss of enzyme activity after six months. |
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Keywords: | Methanol dehydrogenase Purification Methylobacterium extorquens AM1 Cation exchange chromatography |
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