Rhodococcus strains as source for ene-reductase activity

Journal article (2018)

Authors

B. Chen Sun Yat-sen University, BT/Biocatalysis - AS
R. Medici BT/Biocatalysis - AS
M. van der Helm BT/Biocatalysis - AS
Y.A.A. van Zwet BT/Biocatalysis - AS
L. Gjonaj Leiden University Medical Center, BT/Biocatalysis - AS
R.C.S. van der Geest BT/Biocatalysis - AS
L.G. Otten BT/Biocatalysis - AS
U. Hanefeld BT/Biocatalysis - AS
Research Group
BT/Biocatalysis (AS) (TU Delft)
Copyright: © 2018 B. Chen, R. Medici, M. van der Helm, Y.A.A. van Zwet, L. Gjonaj, R.C.S. van der Geest, L.G. Otten, U. Hanefeld
DOI
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https://doi.org/10.1007/s00253-018-8984-7
Rhodococcus Asymmetric reduction Enantioselectivity Ene-reductase
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Published Date

2018

Language

English

Reuse Rights

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Faculty

Applied Sciences

Department

BT/Biotechnologie

Research Group

BT/Biocatalysis

Abstract

Rhodococcus strains are ubiquitous in nature and known to metabolise a wide variety of compounds. At the same time, asymmetric reduction of C=C bonds is important in the production of high-valued chiral building blocks. In order to evaluate if Rhodococci can be used for this task, we have probed several Rhodococcus rhodochrous and R. erythropolis strains for ene-reductase activity. A series of substrates including activated ketones, an aldehyde, an imide and nitro-compound were screened using whole cells of seven Rhodococcus strains. This revealed that whole cells of all Rhodococcus strains showed apparent (S)-selectivity towards ketoisophorone, while most other organisms show (R)-selectivity for this compound. Three putative ene-reductases from R. rhodochrous ATCC 17895 were heterologously expressed in Escherichia coli. One protein was purified and its biocatalytic and biochemical properties were characterised, showing typical (enantioselective) properties for class 3 ene-reductases of the old yellow enzyme family.