A rapid method for the purification of methanol dehydrogenase from Methylobacterium extorquens
Date of Publication
Protein Expression and Purification
Department of Chemistry, The University of Toledo, Toledo, OH
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 °C in 20 mM phosphate buffer, pH 7.0, showed only a negligible loss of enzyme activity after six months.
Liu, Q.; Kirchhoff, J. R.; Faehnle, C. R.; Viola, R. E.; and Hudson, R. A., "A rapid method for the purification of methanol dehydrogenase from Methylobacterium extorquens" (2005). Pharmaceutical Sciences. 1968.