Enzymatic hydrolysis of cyanohydrins with recombinant nitrile hydratase and amidase from hodococcus erythropolis
- 1 November 2004
- journal article
- research article
- Published by Springer Science and Business Media LLC in Biotechnology Letters
- Vol. 26 (21), 1675-1680
- https://doi.org/10.1007/s10529-004-3521-4
Abstract
Nitrile hydratase and amidase from Rhodococcus erythropolis CIMB11540 were both cloned and expressed in Escherichia coli.Crude cell free extracts were used for the hydrolysis of different aromatic cyanohydrins. Nitrile hydratase expression was increased up to 5-fold by redesign of the expression cassette. The recombinant enzymes were successfully used for the conversion of several cyanohydrins to the corresponding α-hydroxy amides and acids while retaining enantiopurity.Keywords
This publication has 17 references indexed in Scilit:
- Biocatalytic hydrolysis of cyanohydrins: an efficient approach to enantiopure α-hydroxy carboxylic acidsJournal of Molecular Catalysis B: Enzymatic, 2003
- Nitrile- and Amide-converting Microbial Enzymes: Stereo-, Regio- and ChemoselectivityBiocatalysis and Biotransformation, 2002
- Cloning and expression of the nitrile hydratase and amidase genes from Bacillus sp. BR449 into Escherichia coliEnzyme and Microbial Technology, 2000
- Nitrile hydrolasesCurrent Opinion in Chemical Biology, 2000
- Crystallization of a photosensitive nitrile hydratase from Rhodococcus sp. N-771Journal of Molecular Biology, 1991
- Cloning and characterization of an amidase gene from Rhodococcus species N-774 and its expression in Escherichia coliBiochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1991
- High efficiency transformation of Escherichia coli with plasmidsGene, 1990
- Nitrile hydratase of Rhodococcus sp. N‐774 Purification and amino acid sequencesFEBS Letters, 1989
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Butyramide-utilizing Mutants of Pseudomonas aeruginosa 8602 which Produce an Amidase with Altered Substrate SpecificityJournal of General Microbiology, 1969