Degradation of D,L-2-chloropropionic Acid by Bacterial Dehalogenases that Shows Stereospecificity and its Partial Enzymatic Characteristics

Research Article

Degradation of D,L-2-chloropropionic Acid by Bacterial Dehalogenases that Shows Stereospecificity and its Partial Enzymatic Characteristics

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.

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S. Thasif, S. Hamdan and F. Huyop, 2009. Degradation of D,L-2-chloropropionic Acid by Bacterial Dehalogenases that Shows Stereospecificity and its Partial Enzymatic Characteristics. Biotechnology, 8: 264-269.

DOI: 10.3923/biotech.2009.264.269

URL: https://scialert.net/abstract/?doi=biotech.2009.264.269

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S. Thasif

S. Hamdan

F. Huyop

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Research Article

Degradation of D,L-2-chloropropionic Acid by Bacterial Dehalogenases that Shows Stereospecificity and its Partial Enzymatic Characteristics

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