Hoyle, A.J. and Bunch, A.W. and Knowles, C.J. (1998) The nitrilases of Rhodococcus rhodochrous NCIMB 11216. Enzyme and Microbial Technology, 23 (7-8). pp. 475-482. ISSN 0141-0229.
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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: | 09 Jul 2009 10:08 |
| Resource URI: | http://kar.kent.ac.uk/id/eprint/17826 (The current URI for this page, for reference purposes) |
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