TY - JOUR
T1 - A rapid method for the purification of methanol dehydrogenase from Methylobacterium extorquens
AU - Liu, Qinfeng
AU - Kirchhoff, J. R.
AU - Faehnle, C. R.
AU - Viola, R. E.
AU - Hudson, R. A.
PY - 2005/8/11
Y1 - 2005/8/11
N2 - 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.
AB - 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.
UR - https://cufind.campbell.edu/pharmacy/1968
UR - https://doi.org/10.1016/j.pep.2005.07.014
U2 - 10.1016/j.pep.2005.07.014
DO - 10.1016/j.pep.2005.07.014
M3 - Article
VL - 46
JO - Protein Expression and Purification
JF - Protein Expression and Purification
ER -