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Title (Primary) Purification and characterization of NAD dependent n-butanol dehydrogenase from solvent tolerant n-butanol degrading Enterobacter sp VKGH12
Author Veeranagouda, Y.; Benndorf, D.; Heipieper, H.J.; Karegoudar, T.B.;
Journal Journal of Microbiology and Biotechnology
Year 2008
Department UBT; PROTEOM;
Volume 18
Issue 4
Language englisch;
Abstract The solvent-tolerant bacterium Enterobacter sp. VKGH12 is capable of utilizing n-butanol and contains an NAD+-dependent n-butanol dehydrogenase (BDH). The BDH from n-butanol-grown Enterobacter sp. was purified from a cell-free extract (soluble fraction) to near homogeneity using a 3-step procedure. The BDH was purified 15.37-fold with a recovery of only 10.51, and the molecular mass estimated to be 38 kDa. The apparent Michaelis-Menten constant (Km) for the BDH was found to be 4 mM with respect to n-butanol. The BDH also had a broad range of substrate specificity, including primary alcohols, secondary alcohols, and aromatic alcohols, and exhibited an optimal activity at pH 9.0 and 40oC. Among the metal ions studied, Mg2+ and Mn2+ had no effect, whereas Cu2+, Zn2+, and Fe2+ at 1 mM completely inhibited the BDH activity. The BDH activity was not inhibited by PMSF, suggesting that serine is not involved in the catalytic site. The known metal ion chelator EDTA had no effect on the BDH activity. Thus, in addition to its physiological significance, some features of the enzyme, such as its activity at an alkaline pH and broad range of substrate specificity, including primary and secondary alcohols, are attractive for application to the enzymatic conversion of alcohols.
ID 1535
Persistent UFZ Identifier https://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=1535
Veeranagouda, Y., Benndorf, D., Heipieper, H.J., Karegoudar, T.B. (2008):
Purification and characterization of NAD dependent n-butanol dehydrogenase from solvent tolerant n-butanol degrading Enterobacter sp VKGH12
J. Microbiol. Biotechnol. 18 (4), 663 - 669