Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 90, Issue -, Pages 17-22Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molcatb.2013.01.010
Keywords
Oceanospirillum sp.; Aldehyde reductase; Bioreduction; Chemoselectivity; Marine enzyme
Funding
- Chinese Academy of Sciences [KGCX2-YW-203, KSCX2-EW-G-14]
- National Key Basic Research and Development Program [2011CB710801]
Ask authors/readers for more resources
A putative aldehyde reductase gene from Oceanospirillum sp. MED92 was overexpressed in Escherichia coli. The recombinant protein (OsAR) was characterized as a monomeric NADPH-dependent aldehyde reductase. The kinetic parameters K-m and k(cat) of OsAR were 0.89 +/- 0.08 mM and 11.07 +/- 0.99 s(-1) for benzaldehyde, 0.04 +/- 0.01 mM and 6.05 +/- 1.56 s(-1) for NADPH, respectively. This enzyme exhibited high activity toward a variety of aromatic and aliphatic aldehydes, but no activity toward ketones. As such, it catalyzed the chemoselective reduction of aldehydes in the presence of ketones, as demonstrated by the reduction of 4-acetylbenzaldehyde or the mixture of hexanal and 2-nonanone, showing the application potential of this marine enzyme in such selective reduction of synthetic importance. (C) 2013 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available