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Published on: January 23, 2019
A rapid method for the purification of methanol dehydrogenase from Methylobacterium extorquens
Qinfeng Liu1, Jon R Kirchhoff, Christopher R Faehnle
1Department of Chemistry, The University of Toledo, Toledo, OH 43606, USA.
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.

