Highly efficient conversion of 1-cyanocycloalkaneacetonitrile using a “super nitrilase mutant” View Full Text


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Article Info

DATE

2018-11-28

AUTHORS

Zhe Xu, Neng Xiong, Shu-Ping Zou, Yu-Xiao Liu, Zhi-Qiang liu, Ya-Ping Xue, Yu-Guo Zheng

ABSTRACT

Nitrilase is the member of carbon–nitrogen hydrogen hydrolase superfamily, which has been widely used for the hydrolysis of nitriles into corresponding carboxylic acids. But most nitrilases are plagued by product inhibition in the industrial application. In this study, a “super nitrilase mutant” of nitrilase with high activity, thermostability and improved product tolerance from Acidovorax facilis ZJB09122 was characterized. Then, an efficient process was developed by employing the whole cell of recombinant E. coli for the conversion of high concentration of 1-cyanocyclohexylacetonitrile-to-1-cyanocyclohexaneacetic acid, an important intermediate of gabapentin. Under the optimized conditions, the higher substrate concentrations such as 1.3 M, 1.5 M and 1.8 M could be hydrolyzed by 13.58 g DCW/L with outstanding productivity (> 740 g/L/day). This study developed a highly efficient bioprocess for the preparation of 1-cyanocyclohexaneacetic acid which has the great potential for industrial application. More... »

PAGES

455-463

References to SciGraph publications

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  • 2011-09-22. A New Nitrilase-Producing Strain Named Rhodobacter sphaeroides LHS-305: Biocatalytic Characterization and Substrate Specificity in APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
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    https://www.ncbi.nlm.nih.gov/pubmed/30488321


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    30 schema:description Nitrilase is the member of carbon–nitrogen hydrogen hydrolase superfamily, which has been widely used for the hydrolysis of nitriles into corresponding carboxylic acids. But most nitrilases are plagued by product inhibition in the industrial application. In this study, a “super nitrilase mutant” of nitrilase with high activity, thermostability and improved product tolerance from Acidovorax facilis ZJB09122 was characterized. Then, an efficient process was developed by employing the whole cell of recombinant E. coli for the conversion of high concentration of 1-cyanocyclohexylacetonitrile-to-1-cyanocyclohexaneacetic acid, an important intermediate of gabapentin. Under the optimized conditions, the higher substrate concentrations such as 1.3 M, 1.5 M and 1.8 M could be hydrolyzed by 13.58 g DCW/L with outstanding productivity (> 740 g/L/day). This study developed a highly efficient bioprocess for the preparation of 1-cyanocyclohexaneacetic acid which has the great potential for industrial application.
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