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Title: Purification and properties of Rhizobial DehL expressed in Escherichia coli
Authors: Huyop, F.
Rashid, N. A.
Wahab, R. A. B.
Cooper, Ronald A.
First Published: 17-Jun-2008
Publisher: Academic Journals
Citation: African Journal of Biotechnology Vol. 7 (12), pp. 1944-1949, 17 June, 2008
Abstract: The Rhizobium sp. DehL was produced by heterologous expression of the cloned gene in Escherichia coli. DehL enzyme was purified to homogeneity and characterized. The molecular weights were estimated to be 61 and 31 kDa by gel filtration and SDS-polyacrylamide gel electrophoresis (SDS-PAGE), respectively, suggesting that the enzyme is a dimer. The purified enzyme was specific to the L-isomer monochloropropionate (L-2CP) and dichloroacetate (DCA). This protein was not able to act on 2,2-dichloropropionate (2,2DCP) and trichloroacetate (TCA). The estimated kinetic data indicated that this enzyme has high affinity to its specific substrates. By searching protein amino acid sequence database, the predicted amino acid sequence of DehL showed a high level of homology to those L-specific monochloropropionate (D,L-2CP) dehalogenase of Rhizobiumsp. NHG3 with 53% sequence identity. The amino acid sequence of DehL showed low level sequence identity to those of Class 1D dehalogenases, suggesting DehL from Rhizobium sp. may belong to different group of dehalogenase classification preferably Class 1L dehalogenase.
DOI Link: 10.5897/AJB2008.000-5041
ISSN: 1684-5315
eISSN: 1684-5315
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © 2008 Author(s) retain the copyright of this article. This article is published under the terms of the Creative Commons Attribution License 4.0 CC BY 4.0
Appears in Collections:Published Articles, Dept. of Biochemistry

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