Enzymatic dehalogenation of 2,2-dichloropropionic acid by locally isolated methylobacterium sp. HJ1

Synthetic halogenated organic compounds are found widely throughout the biosphere due to modern industrial and agricultural processes. Various soils microorganisms are able to utilize halogenated alkanoic acids as a sole carbon source. An active dehalogenase enzyme was demonstrated in the crude extr...

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Main Authors: Jing, Ng Hong, Huyop, Fahrul
Format: Article
Published: Asian Network for Scientific Information 2008
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author Jing, Ng Hong
Huyop, Fahrul
author_facet Jing, Ng Hong
Huyop, Fahrul
author_sort Jing, Ng Hong
collection ePrints
description Synthetic halogenated organic compounds are found widely throughout the biosphere due to modern industrial and agricultural processes. Various soils microorganisms are able to utilize halogenated alkanoic acids as a sole carbon source. An active dehalogenase enzyme was demonstrated in the crude extracts of partially purified enzyme from Methylobacterium sp. HJ1. The ability of the enzyme to catalyze the dehalogenation of various halogen-substituted organic acids was investigated and the highest activity was found with 2,2-dichloropropionic acid with maximum activity in phosphate buffer pH 6.8. The partially purified enzyme was unaffected by Co+, Mg+ or Mn+ ions or glutathione. The enzyme removed chlorides ions present on a number of 2-carbon alkanoic acids if the halogen was on the a but not on the ß-position. The putative product of dehalogenation was pyruvate using a standard assay system and at the same time 2,2-dichloropropionic acid depletion was detected in growth medium by High Performance Liquid Chromatography (HPLC).
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spelling utm.eprints-128362011-06-30T10:10:54Z http://eprints.utm.my/12836/ Enzymatic dehalogenation of 2,2-dichloropropionic acid by locally isolated methylobacterium sp. HJ1 Jing, Ng Hong Huyop, Fahrul Q Science (General) Synthetic halogenated organic compounds are found widely throughout the biosphere due to modern industrial and agricultural processes. Various soils microorganisms are able to utilize halogenated alkanoic acids as a sole carbon source. An active dehalogenase enzyme was demonstrated in the crude extracts of partially purified enzyme from Methylobacterium sp. HJ1. The ability of the enzyme to catalyze the dehalogenation of various halogen-substituted organic acids was investigated and the highest activity was found with 2,2-dichloropropionic acid with maximum activity in phosphate buffer pH 6.8. The partially purified enzyme was unaffected by Co+, Mg+ or Mn+ ions or glutathione. The enzyme removed chlorides ions present on a number of 2-carbon alkanoic acids if the halogen was on the a but not on the ß-position. The putative product of dehalogenation was pyruvate using a standard assay system and at the same time 2,2-dichloropropionic acid depletion was detected in growth medium by High Performance Liquid Chromatography (HPLC). Asian Network for Scientific Information 2008 Article PeerReviewed Jing, Ng Hong and Huyop, Fahrul (2008) Enzymatic dehalogenation of 2,2-dichloropropionic acid by locally isolated methylobacterium sp. HJ1. Journal of Biological Sciences, 8 (1). pp. 233-235. ISSN 17273048
spellingShingle Q Science (General)
Jing, Ng Hong
Huyop, Fahrul
Enzymatic dehalogenation of 2,2-dichloropropionic acid by locally isolated methylobacterium sp. HJ1
title Enzymatic dehalogenation of 2,2-dichloropropionic acid by locally isolated methylobacterium sp. HJ1
title_full Enzymatic dehalogenation of 2,2-dichloropropionic acid by locally isolated methylobacterium sp. HJ1
title_fullStr Enzymatic dehalogenation of 2,2-dichloropropionic acid by locally isolated methylobacterium sp. HJ1
title_full_unstemmed Enzymatic dehalogenation of 2,2-dichloropropionic acid by locally isolated methylobacterium sp. HJ1
title_short Enzymatic dehalogenation of 2,2-dichloropropionic acid by locally isolated methylobacterium sp. HJ1
title_sort enzymatic dehalogenation of 2 2 dichloropropionic acid by locally isolated methylobacterium sp hj1
topic Q Science (General)
work_keys_str_mv AT jingnghong enzymaticdehalogenationof22dichloropropionicacidbylocallyisolatedmethylobacteriumsphj1
AT huyopfahrul enzymaticdehalogenationof22dichloropropionicacidbylocallyisolatedmethylobacteriumsphj1