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dc.contributor.authorJing, Ng Hong
dc.contributor.authorSulaiman, Fatin Hanani
dc.contributor.authorWahab, Roswanira Ab.
dc.contributor.authorPakingking, Rolando V., Jr.
dc.contributor.authorRashid, Noor Aini Abdul
dc.contributor.authorHuyop, Fahrul
dc.date.accessioned2014-05-22T08:49:40Z
dc.date.available2014-05-22T08:49:40Z
dc.date.issued2008
dc.identifier.citationJing, N. H., Sulaiman, F. H., Wahab, R. A., Pakingking Jr., R. V., 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.en
dc.identifier.issn1996-0808
dc.identifier.urihttp://hdl.handle.net/10862/2081
dc.description.abstractThe 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.en
dc.language.isoenen
dc.publisherAcademic Journalsen
dc.relation.urihttp://www.academicjournals.org/article/article1380107277_Jing%20et%20al.pdf
dc.subjectpyruvatesen
dc.titlePurification and properties of a non-stereospecific dehalogenase enzyme E (DehE) from Methylobacterium sp. HJ1en
dc.typeArticleen
dc.citation.volume2
dc.citation.issue7
dc.citation.spage187
dc.citation.epage191
dc.citation.journalTitleAfrican Journal of Microbiology Researchen
dc.subject.asfacarbonen
dc.subject.asfamolecular weighten
dc.subject.asfaproteinsen
dc.subject.asfaenzymesen
dc.subject.asfachloridesen
dc.subject.asfaacidsen
dc.subject.asfamicroorganismsen
dc.subject.asfaweighten
dc.subject.asfaelectrophoresisen


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  • AQD Journal Articles [1213]
    These papers were contributed by AQD staff to various national and international journals

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