Dehalogennation of Halokanes by Rhodococuus-Erythropolis Y2

Armfield, Susan J. and Sallis, Paul J. and Baker, Peter B. and Bull, Alan T. and Hardman, David J. (1995) Dehalogennation of Halokanes by Rhodococuus-Erythropolis Y2. Biodegradation, 6 (3). pp. 237-246. ISSN 0923-9820. (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)

The full text of this publication is not available from this repository. (Contact us about this Publication)
Official URL


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
Subjects: T Technology > T Technology (General)
Divisions: Faculties > Science Technology and Medical Studies > School of Engineering and Digital Arts
Depositing User: P. Ogbuji
Date Deposited: 08 Jun 2009 18:27
Last Modified: 08 May 2014 09:45
Resource URI: (The current URI for this page, for reference purposes)
  • Depositors only (login required):


Downloads per month over past year