Huyop, F. and Thasif, S. and Hamdan, S. (2009) Degradation of D,L-2-chloropropionic acid by bacterial dehalogenases that shows stereospecificity and its partial enzymatic characteristics. Biotechnology(Faisalabad), 8 (2). pp. 264-269. ISSN 1682296X
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Official URL: http://dx.doi.org/10.3923/biotech.2009.264.269
A Pseudomonas sp. strain S3, which can utilise a halogenated compound of D., L-2CP as sole carbon and energy source, catalyses the hydrolytic dehalogenation of both D-and L-isomers of 2-chloropropionic acid. Two kinds of dehalogenase enzymes were isolated from cells of Pseudomonas sp. strain S3. A thermostable L-specific dehalogenase (DehL) and non-thermostable D-specific dehalogenase (DehD) can be obtained when cells grown only in the presence of D., L-2CP. These inducible enzymes were then further characterised. The maximum activity of D-specific dehalogenase (DehD) enzyme on D-2CP was found at pH 9.5 at 35°C, whereas the L-specific dehalogenase is thermostable and retained its full activity upon heating at 55°C for 15 min. The pH and temperature optima for dehalogenation of L-2CP were 7.5 and 50°C. respectively.
|Uncontrolled Keywords:||2-Chloropropionic acid, degradation, dehalogenase, enzymatic characteristics|
|Subjects:||T Technology > T Technology (General)|
|Divisions:||Biosciences and Bioengineering (Formerly known)|
|Deposited By:||Ms Zalinda Shuratman|
|Deposited On:||03 Aug 2011 07:07|
|Last Modified:||03 Aug 2011 07:07|
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