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

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