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

Jing, Ng Hong and Sulaiman, Fatin Hanani and Ab. Wahab, Roswanira and Pakinging, Rolando V., Jr. and Abdul Rashid, Noor Aini and Huyop, Fahrul (2008) Purification and properties of a non-stereospecific dehalogenase enzyme E (DehE) from Methylobacterium sp HJ1. African Journal Of Microbiology Research, 2 (7). pp. 187-191. ISSN 1996-0808

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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 K-m value for the hydrolysis of 2, 2-dichloropropionic acid was 0.25 mM. The enzyme removes chloride present on the -position, but not on the -position, of a number 2-carbon alkanoic acids.

Item Type:Article
Uncontrolled Keywords:haloalkanoic acid, dichloropropionate, 2, 2-dichloropropionic acid
Subjects:Q Science > Q Science (General)
Divisions:Biosciences and Bioengineering (Formerly known)
ID Code:12856
Deposited By: Liza Porijo
Deposited On:04 Jul 2011 01:30
Last Modified:04 Jul 2011 01:30

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