Title
A rapid method for the purification of methanol dehydrogenase from Methylobacterium extorquens
Document Type
Article
Date of Publication
8-11-2005
Publication Title
Protein Expression and Purification
First Page
316
Last Page
320
Location
Department of Chemistry, The University of Toledo, Toledo, OH
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 °C in 20 mM phosphate buffer, pH 7.0, showed only a negligible loss of enzyme activity after six months.
DOI
https://doi.org/10.1016/j.pep.2005.07.014
Recommended Citation
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.
https://cufind.campbell.edu/pharmacy/1968
