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Purification and properties of a non-stereospecific dehalogenase enzyme E (DehE) from Methylobacterium sp. HJ1

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www.academicjournals.org
Date
2008
Author
Jing, Ng Hong
Sulaiman, Fatin Hanani
Wahab, Roswanira Ab.
Pakingking, Rolando V., Jr. ORCID
Rashid, Noor Aini Abdul
Huyop, Fahrul
Page views
863
ASFA keyword
carbon ASFA
molecular weight ASFA
proteins ASFA
enzymes ASFA
chlorides ASFA
acids ASFA
microorganisms ASFA
weight ASFA
electrophoresis ASFA
AGROVOC keyword
pyruvates AGROVOC
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Abstract
The bacterial isolate HJ1, which was identified as a Methylobacterium sp., grew on 2, 2-dichloropropionic acid as the sole carbon source and produced a 2-haloalkanoic acid hydrolytic dehalogenase. This non-stereospecific dehalogenase E (DehE) catalysed the hydrolytic dechlorination of 2, 2-dichloropropionic acid and D, L-2-chloropropionic acid to produce pyruvate and lactate, respectively. The enzyme was purified to homogeneity and characterized. The molecular weight was 36 kDa by SDS-polyacrylamide gel electrophoresis and 72 kDa by gel filtration, suggesting that the enzyme is a protein dimer. The purified enzyme was only inhibited by HgSO4 and was non-stereospecific to haloalkanoic acids. The Km value for the hydrolysis of 2, 2-dichloropropionic acid was 0.25 mM. The enzyme removes chloride present on the α-position, but not on the β-position, of a number 2-carbon alkanoic acids.
URI
http://hdl.handle.net/10862/2081
Suggested Citation
Jing, N. H., Sulaiman, F. H., Wahab, R. A., Pakingking, R. V., Jr., Rashid, N. A. A., & Huyop, F. (2008). Purification and properties of a non-stereospecific dehalogenase enzyme E (DehE) from Methylobacterium sp. HJ1. African Journal of Microbiology Research, 2(7), 187-191. http://hdl.handle.net/10862/2081
Type
Article
ISSN
1996-0808
Collections
  • Journal Articles [1183]


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