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Dehalogennation of Halokanes by Rhodococuus-Erythropolis Y2

Armfield, Susan J., Sallis, Paul J., Baker, Peter B., Bull, Alan T., Hardman, David J. (1995) Dehalogennation of Halokanes by Rhodococuus-Erythropolis Y2. Biodegradation, 6 (3). pp. 237-246. ISSN 0923-9820. (doi:10.1007/BF00700463) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:19674)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL:
http://dx.doi.org/10.1007/BF00700463

Abstract

Rhodococcus erythropolis Y2 produced two types of dehalogenase: a hydrolytic enzyme, that is an halidohydrolase, which was induced by C-3 to C-6 1-haloalkane substrates, and at least one oxygenase-type dehalogenase induced by C-7 to C-16 1-haloalkanes and n-alkanes. The oxygenase-type activity dehalogenated C-4 to C-18 1-chloroalkanes with an optimum activity towards 1-chlorotetradecane, The halidohydrolase catalysed the dehalogenation of a wide range of 1- and alpha,omega-disubstituted haloalkanes and alpha,omega-substituted haloalcohols. In resting cell suspensions of hexadecane-grown R. erythropolis Y2 the oxygenase-type dehalogenase had a specific activity of 12.9 mU (mg protein)(-1) towards 1-chlorotetradecane (3.67 mU mg(-1) towards 1-chlorobutane) whereas the halidohydrolase in 1-chlorobutane-grown batch cultures had a specific activity of 44 mU (mg protein)(-1) towards 1-chlorobutane. The significance of the two dehalogenase systems in a single bacterial strain is discussed in terms of their contribution to the overall catabolic potential of the organism.

Item Type: Article
DOI/Identification number: 10.1007/BF00700463
Uncontrolled keywords: HALOALKANE; HALIDOHYDROLASE; OXYGENASE
Subjects: T Technology > T Technology (General)
Divisions: Divisions > Division of Computing, Engineering and Mathematical Sciences > School of Engineering and Digital Arts
Depositing User: P. Ogbuji
Date Deposited: 08 Jun 2009 18:27 UTC
Last Modified: 16 Nov 2021 09:57 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/19674 (The current URI for this page, for reference purposes)

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