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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my.utm.128362011-06-30T10:10:54Z http://eprints.utm.my/id/eprint/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 |
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Q Science (General) Jing, Ng Hong Huyop, Fahrul Enzymatic dehalogenation of 2,2-dichloropropionic acid by locally isolated methylobacterium sp. HJ1 |
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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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Article |
author |
Jing, Ng Hong Huyop, Fahrul |
author_facet |
Jing, Ng Hong Huyop, Fahrul |
author_sort |
Jing, Ng Hong |
title |
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_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_sort |
enzymatic dehalogenation of 2,2-dichloropropionic acid by locally isolated methylobacterium sp. hj1 |
publisher |
Asian Network for Scientific Information |
publishDate |
2008 |
url |
http://eprints.utm.my/id/eprint/12836/ |
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1643646052698423296 |
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13.201949 |