Journal
CHEMCATCHEM
Volume 7, Issue 2, Pages 271-275Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cctc.201402877
Keywords
biotransformations; enzyme catalysis; hydrolysis; immobilization; nitrilases
Categories
Funding
- Chinese Academy of Sciences [KSZD-EW-015]
- CAS Agenda to Provide S&T Support and Services for National Strategic Emerging Industries
- National Natural Science Foundation of China [21302215]
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An enzymatic method for the synthesis of ethyl (R)-3-hydroxyglutarate from ethyl (R)-4-cyano-3-hydroxybutyate was developed by using free and immobilized recombinant Escherichia coli BL21(DE3)pLysS harboring a nitrilase gene from Arabidopsis thaliana (AtNIT2). The hydrolysis of ethyl (R)-4-cyano-3-hydroxybutyate proceeded with the freely suspended cells of the biocatalyst under the optimized conditions of 1.5 mol L-1 (235.5 g L-1) substrate concentration and 6.0 wt% loading of wet cells at pH 8.0 and 25 degrees C, with 100% conversion obtained in 4.5 h. Furthermore, immobilization of the whole cells enhanced their substrate tolerance, stability, and reusability. Under the optimized conditions (100 mmol L-1 tris(hydroxymethyl) aminomethane hydrochloride buffer, pH 8.0, 25 degrees C), the immobilized biocatalyst could be reused for up to 16 batches, with a biocatalyst productivity of 55.6 gg(wet) (-1)(cells) and a space-time productivity of 625.5 g L-1 d(-1). These results demonstrated that the immobilized whole cells might be used as a biocatalyst in the industrial production of ethyl (R)-3-hydroxyglutarate, a key intermediate for the synthesis of rosuvastatin.
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