Armfield, S.J. and Sallis, P.J. and Baker, P.B. and Bull, A.T. and Hardman, D.J. (1995) Dehalogennation of Halokanes by Rhodococuus-Erythropolis Y2. Biodegradation, 6 (3). pp. 237-246. ISSN 0923-9820.
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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.
|Uncontrolled keywords:||HALOALKANE; HALIDOHYDROLASE; OXYGENASE|
|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:||13 Jun 2012 09:40|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/19674 (The current URI for this page, for reference purposes)|
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