The nitrilases of Rhodococcus rhodochrous NCIMB 11216

Hoyle, Alison J. and Bunch, Alan William and Knowles, Christopher J. (1998) The nitrilases of Rhodococcus rhodochrous NCIMB 11216. Enzyme and Microbial Technology, 23 (7-8). pp. 475-482. ISSN 0141-0229. (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1016/S0141-0229(98)00076-3

Abstract

Rhodococcus rhodochrous NCIMB 11216 grows on propionitrile or benzonitrile as the sole source of carbon and nitrogen. The possibility that different nitrile-hydrolyzing enzymes were produced under these two growth conditions was investigated. Nitrilase activity in whole cell suspensions from either bacteria grown on propionitrile or benzonitrile were capable of biotransforming a wide range of nitriles. The propionitrile-induced nitrile degrading activity hydrolyzed 3-cyanobenzoate and both the nitrile groups in 1,3-dicyanobenzoate. In contrast, the benzonitrile-induced activity hydrolyzed only one of the nitrile groups in 1,3-dicyanobenzoate, but did not affect 3-cyanobenzoate. Both nitrilases biotransformed alpha-cyano-o-tolunitrile to produce 2-cyanophenylacetic acid. The nitrilases were purified by fast protein liquid chromatography and the iv-terminus of each enzyme sequenced. SDS-PAGE analysis identified a subunit molecular weight of 45.8 kDa for each nitrilase. The N-terminal sequences showed significant similarity with other sequenced nitrilases and with the exception of a single amino acid were identical with each other. Both nitrilases had temperature and pH optima of 30 degrees C and 8.0, respectively. The propionitrile-induced nitrilase had a K-m for benzonitrile of 20.7 mM and a V-max of 12.4 mu mol min(-1) mg(-1) protein whereas the benzonitrile-induced nitrilase had a K-m for benzonitrile of 8.83 mM and a V-max of 0.57 mu mol min(-1) mg(-1) protein.

Item Type: Article
Subjects: Q Science > QR Microbiology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: R.F. Xu
Date Deposited: 09 Jul 2009 10:08
Last Modified: 28 May 2014 10:30
Resource URI: http://kar.kent.ac.uk/id/eprint/17826 (The current URI for this page, for reference purposes)
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