A further characterization of 3-chloropropionic acid dehalogenase from rhodococcus sp. HJ1
The main aim of the present study is to further characterize a new dehalogenase enzyme found in the crude extracts from Rhodococcus sp. The ability of the enzyme to catalyze the dehalogenation of various halogen-substituted organic acids was investigated and the highest activity was found with 3-chl...
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2009
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my.utm.146652020-06-15T03:46:27Z http://eprints.utm.my/id/eprint/14665/ A further characterization of 3-chloropropionic acid dehalogenase from rhodococcus sp. HJ1 Jing, Ng Hong Ab. Wahab, Roswanira Mohd. Taha, Aishah Abdul Rashid, Noor Aini Huyop, Fahrul Q Science (General) TA Engineering (General). Civil engineering (General) The main aim of the present study is to further characterize a new dehalogenase enzyme found in the crude extracts from Rhodococcus sp. The ability of the enzyme to catalyze the dehalogenation of various halogen-substituted organic acids was investigated and the highest activity was found with 3-chloropropionic acid as a sole carbon source in the growth medium. The enzyme followed Michaelis-Menten kinetics and the Km for 3-chloropropionic acid was 0.2 mM. Maximum activity was found at pH 7.6 at 30°C. The enzyme activity in the cell-free extract was unaffected by diaminoethane tetraacetic acid (EDTA), dithiothreitol (DTT) or by Mn and Zn ions but was reduced by HgCl2 (70%) and Pb(NO3)2 (80%). The enzyme removed the chlorine atom present on a number of 3- and 4-carbon alkanoic acids if the halogen was on the β-position. 2009-04 Conference or Workshop Item PeerReviewed Jing, Ng Hong and Ab. Wahab, Roswanira and Mohd. Taha, Aishah and Abdul Rashid, Noor Aini and Huyop, Fahrul (2009) A further characterization of 3-chloropropionic acid dehalogenase from rhodococcus sp. HJ1. In: International Congress of Malaysian Society for Microbiology (ICMSM 2009), 2009, Park Royal Hotel, Pulau Pinang. http://dx.doi.org/10.3923/jm.2008.482.488 |
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Q Science (General) TA Engineering (General). Civil engineering (General) Jing, Ng Hong Ab. Wahab, Roswanira Mohd. Taha, Aishah Abdul Rashid, Noor Aini Huyop, Fahrul A further characterization of 3-chloropropionic acid dehalogenase from rhodococcus sp. HJ1 |
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The main aim of the present study is to further characterize a new dehalogenase enzyme found in the crude extracts from Rhodococcus sp. The ability of the enzyme to catalyze the dehalogenation of various halogen-substituted organic acids was investigated and the highest activity was found with 3-chloropropionic acid as a sole carbon source in the growth medium. The enzyme followed Michaelis-Menten kinetics and the Km for 3-chloropropionic acid was 0.2 mM. Maximum activity was found at pH 7.6 at 30°C. The enzyme activity in the cell-free extract was unaffected by diaminoethane tetraacetic acid (EDTA), dithiothreitol (DTT) or by Mn and Zn ions but was reduced by HgCl2 (70%) and Pb(NO3)2 (80%). The enzyme removed the chlorine atom present on a number of 3- and 4-carbon alkanoic acids if the halogen was on the β-position. |
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Conference or Workshop Item |
author |
Jing, Ng Hong Ab. Wahab, Roswanira Mohd. Taha, Aishah Abdul Rashid, Noor Aini Huyop, Fahrul |
author_facet |
Jing, Ng Hong Ab. Wahab, Roswanira Mohd. Taha, Aishah Abdul Rashid, Noor Aini Huyop, Fahrul |
author_sort |
Jing, Ng Hong |
title |
A further characterization of 3-chloropropionic acid dehalogenase from rhodococcus sp. HJ1 |
title_short |
A further characterization of 3-chloropropionic acid dehalogenase from rhodococcus sp. HJ1 |
title_full |
A further characterization of 3-chloropropionic acid dehalogenase from rhodococcus sp. HJ1 |
title_fullStr |
A further characterization of 3-chloropropionic acid dehalogenase from rhodococcus sp. HJ1 |
title_full_unstemmed |
A further characterization of 3-chloropropionic acid dehalogenase from rhodococcus sp. HJ1 |
title_sort |
further characterization of 3-chloropropionic acid dehalogenase from rhodococcus sp. hj1 |
publishDate |
2009 |
url |
http://eprints.utm.my/id/eprint/14665/ http://dx.doi.org/10.3923/jm.2008.482.488 |
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1672610420551057408 |
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13.214268 |