Purification and characterization of a novel p,p’-DDT dehalogenase from Aeromonas sp. strain MY1
Although dichlorodiphenyltrichloroethane (DDT) occupies a prominent position for its recalcitrance in the environment which led to its ban by the Stockholm Convention. This pesticide is still unregulated used in low and middle-income countries, which contributes to the global burden of this hazardo...
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Format: | Article |
Language: | English |
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Joint Coordination Centre of the World Bank assisted National Agricultural Research Programme (NARP)
2021-02-01
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Series: | Journal of Applied Sciences and Environmental Management |
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Online Access: | https://www.ajol.info/index.php/jasem/article/view/203986 |
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author | Y. Murtala B.C. Nwanguma L.U.S. Ezeanyika |
author_facet | Y. Murtala B.C. Nwanguma L.U.S. Ezeanyika |
author_sort | Y. Murtala |
collection | DOAJ |
description |
Although dichlorodiphenyltrichloroethane (DDT) occupies a prominent position for its recalcitrance in the environment which led to its ban by the Stockholm Convention. This pesticide is still unregulated used in low and middle-income countries, which contributes to the global burden of this hazardous contaminant. In the recent time, biological approach has been proven to be effective and environmentally safer for the decontamination of the residual DDT. In this research, we reported a gel-purified p,p’-DDT dehalogenase from Aeromonas sp. strain MY1, revealing a single band with a molecular weight of approximately 37 kDa. The dehalogenase was unique for its capability to release chloride ions from p, p’-DDT substrate with optimum dechlorination activity at pH 8.0 and 35°C. The enzyme followed Michaelis-Menten’s kinetics and measurement of its initial velocities with various p,p’-DDT concentrations showed a Km of 27.05 μmol L-1 and Vmax of 476.19 μmol L-1 min-1. However, the enzyme lost its dechlorination activity in the presence of Ag2+ and Hg2+ This dehalogenase could pave a way for the effective decontamination of p,p’- DDT contaminated environment, suggesting its potentials for p,p’-DDT bio-cleansing applications.
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first_indexed | 2024-04-24T14:51:27Z |
format | Article |
id | doaj.art-8f72ecb5349e41fd9baa4c7615232d1a |
institution | Directory Open Access Journal |
issn | 2659-1502 2659-1499 |
language | English |
last_indexed | 2024-04-24T14:51:27Z |
publishDate | 2021-02-01 |
publisher | Joint Coordination Centre of the World Bank assisted National Agricultural Research Programme (NARP) |
record_format | Article |
series | Journal of Applied Sciences and Environmental Management |
spelling | doaj.art-8f72ecb5349e41fd9baa4c7615232d1a2024-04-02T19:48:37ZengJoint Coordination Centre of the World Bank assisted National Agricultural Research Programme (NARP)Journal of Applied Sciences and Environmental Management2659-15022659-14992021-02-01241210.4314/jasem.v24i12.15Purification and characterization of a novel p,p’-DDT dehalogenase from Aeromonas sp. strain MY1Y. MurtalaB.C. NwangumaL.U.S. Ezeanyika Although dichlorodiphenyltrichloroethane (DDT) occupies a prominent position for its recalcitrance in the environment which led to its ban by the Stockholm Convention. This pesticide is still unregulated used in low and middle-income countries, which contributes to the global burden of this hazardous contaminant. In the recent time, biological approach has been proven to be effective and environmentally safer for the decontamination of the residual DDT. In this research, we reported a gel-purified p,p’-DDT dehalogenase from Aeromonas sp. strain MY1, revealing a single band with a molecular weight of approximately 37 kDa. The dehalogenase was unique for its capability to release chloride ions from p, p’-DDT substrate with optimum dechlorination activity at pH 8.0 and 35°C. The enzyme followed Michaelis-Menten’s kinetics and measurement of its initial velocities with various p,p’-DDT concentrations showed a Km of 27.05 μmol L-1 and Vmax of 476.19 μmol L-1 min-1. However, the enzyme lost its dechlorination activity in the presence of Ag2+ and Hg2+ This dehalogenase could pave a way for the effective decontamination of p,p’- DDT contaminated environment, suggesting its potentials for p,p’-DDT bio-cleansing applications. https://www.ajol.info/index.php/jasem/article/view/203986Aeromonas sp.pp'-DDTdehalogenasebioremediationhalogenated aromatic contaminants |
spellingShingle | Y. Murtala B.C. Nwanguma L.U.S. Ezeanyika Purification and characterization of a novel p,p’-DDT dehalogenase from Aeromonas sp. strain MY1 Journal of Applied Sciences and Environmental Management Aeromonas sp. p p'-DDT dehalogenase bioremediation halogenated aromatic contaminants |
title | Purification and characterization of a novel p,p’-DDT dehalogenase from Aeromonas sp. strain MY1 |
title_full | Purification and characterization of a novel p,p’-DDT dehalogenase from Aeromonas sp. strain MY1 |
title_fullStr | Purification and characterization of a novel p,p’-DDT dehalogenase from Aeromonas sp. strain MY1 |
title_full_unstemmed | Purification and characterization of a novel p,p’-DDT dehalogenase from Aeromonas sp. strain MY1 |
title_short | Purification and characterization of a novel p,p’-DDT dehalogenase from Aeromonas sp. strain MY1 |
title_sort | purification and characterization of a novel p p ddt dehalogenase from aeromonas sp strain my1 |
topic | Aeromonas sp. p p'-DDT dehalogenase bioremediation halogenated aromatic contaminants |
url | https://www.ajol.info/index.php/jasem/article/view/203986 |
work_keys_str_mv | AT ymurtala purificationandcharacterizationofanovelppddtdehalogenasefromaeromonasspstrainmy1 AT bcnwanguma purificationandcharacterizationofanovelppddtdehalogenasefromaeromonasspstrainmy1 AT lusezeanyika purificationandcharacterizationofanovelppddtdehalogenasefromaeromonasspstrainmy1 |