Journal
PROCESS BIOCHEMISTRY
Volume 45, Issue 6, Pages 887-891Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.procbio.2010.02.011
Keywords
Alcaligenes sp.; Nitrilase; Enantioselective; Highly substrate/product tolerable; (R)-(-)-Mandelic acid; Fed-batch reaction
Categories
Funding
- National Natural Science Foundation of China [20672037, 20773038, 20902023]
- Ministry of Science and Technology, PR China [2009ZX09501-016, 2009CB724706]
- China National Special Fund for State Key Laboratory of Bioreactor Engineering [2060204]
- Shanghai Municipal Fund for Natural Science [07ZR14030]
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For efficient production of (R)-(-)-mandelic acid, a nitrilase gene from Alcaligenes sp. ECU0401 was cloned and overexpressed in Escherichia coli. After simple optimization of the culture conditions, the biocatalyst production was greatly increased from 500 to 7000 U/l. The recombinant E. coli whole cells showed strong tolerance against a high substrate concentration of up to 200 mM, and the concentration of (R)-(-)-mandelic acid after only 411 of transformation reached 197 mM with an enantiomeric excess (ee(p)) of 99%. In a fed-batch reaction with 600 mM mandelonitrile as the substrate, the cumulative production of (R)-(-)-mandelic acid after 17.5 h of conversion reached 520 mM. The recombinant E. coli cells could also be repeatedly used in the biotransformation, retaining 40% of the initial activity after 10 batches of reaction. The highly substrate/product tolerable and enantioselective nature of this recombinant nitrilase suggests that it is of great potential for the practical production of optically pure (R)-(-)-mandelic acid. (C) 2010 Elsevier Ltd. All rights reserved.
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