Journal
ENZYME AND MICROBIAL TECHNOLOGY
Volume 77, Issue -, Pages 68-77Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.enzmictec.2015.06.004
Keywords
Aldo-keto reductase; Kluyveromyces lactis; Characterization; Asymmetric bioreduction; Chiral alcohol
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Funding
- National Basic Research Program of China (973 Program) [2011CB710800]
- Major Program for Key Science and Technology of Zhejiang Province of China [2014C03010]
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An aldo-keto reductase gene (klakr) from Kluyveromyces lactis XP1461 was cloned and heterologously expressed in Escherichia coli. The aldo-keto reductase KlAKR was purified and found to be NADH-dependent with a molecular weight of approximately 36 kDa. It is active and stable at 30 degrees C and pH 7.0. The maximal reaction rate (v(max)), apparent Michaelis-Menten constant (K-m) for NADH and t-butyl 6-cyano-(5R)-hydroxy-3-oxohexanoate (1a) and catalytic number (k(cat)) were calculated as 7.63 U mg(-1), 0.204 mM, 4.42 mM and 697.4min(-1), respectively. Moreover, the KlAKR has broad substrate specificity to a range of aldehydes, ketones and keto-esters, producing chiral alcohol with e.e. or d.e. >99% for the majority of test substrates. (C) 2015 Elsevier Inc. All rights reserved.
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