Kinetic studies of the partially purified molybdenum-reducing enzyme from Bacillus pumilus strain Lbna

Bacterial based remediation of environmental toxicants is a promising innovative technology for molybdenum pollution. To date, the enzyme responsible for molybdate reduction to Mo-blue from bacteria show that the Michaelis-Menten constants varies by one order of magnitude. It is important that the c...

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Main Authors: Abo-Shakeer, Lubna Kamil Abdulhussein, Abdul Rahman, Mohd Fadhil, Yakasai, Mohd Hafeez, Abu Bakar, Nurlizah, Othman, Ahmad Razi, Syed, Mohd Arif, Abdullah, Norhani, Abd. Shukor, Mohd. Yunus
Format: Article
Language:English
Published: Hibiscus Publisher 2017
Online Access:http://psasir.upm.edu.my/id/eprint/64017/1/Kinetic%20studies%20of%20the%20partially%20purified%20molybdenum-reducing%20enzyme%20from%20Bacillus%20pumilus%20strain%20Lbna.pdf
http://psasir.upm.edu.my/id/eprint/64017/
https://journal.hibiscuspublisher.com/index.php/BSTR/article/view/354
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spelling my.upm.eprints.640172018-06-08T00:52:04Z http://psasir.upm.edu.my/id/eprint/64017/ Kinetic studies of the partially purified molybdenum-reducing enzyme from Bacillus pumilus strain Lbna Abo-Shakeer, Lubna Kamil Abdulhussein Abdul Rahman, Mohd Fadhil Yakasai, Mohd Hafeez Abu Bakar, Nurlizah Othman, Ahmad Razi Syed, Mohd Arif Abdullah, Norhani Abd. Shukor, Mohd. Yunus Bacterial based remediation of environmental toxicants is a promising innovative technology for molybdenum pollution. To date, the enzyme responsible for molybdate reduction to Mo-blue from bacteria show that the Michaelis-Menten constants varies by one order of magnitude. It is important that the constants from newer enzyme sources be characterized so that a comparison can be made. The aim of this study is to characterize kinetically the enzyme from a previously isolated Mo-reducing bacterium; Bacillus pumilus strain Lbna. The maximum activity of this enzyme occurred at pH 5.5 and in between 25 and 35 °C. The Km and Vmax of NADH were 6.646 mM and 0.057 unit/mg enzyme, while the Km and Vmax of LPPM were 3.399 mM and 0.106 unit/mg enzyme. The results showed that the enzyme activity for Bacillus pumilus strain Lbna were inhibited by all heavy metals used. Zinc, copper, silver, chromium, cadmium and mercury all caused more than 50% inhibition to the Mo-reducing enzyme activity with copper being the most potent with an almost complete inhibition of enzyme activity observed. Hibiscus Publisher 2017 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/64017/1/Kinetic%20studies%20of%20the%20partially%20purified%20molybdenum-reducing%20enzyme%20from%20Bacillus%20pumilus%20strain%20Lbna.pdf Abo-Shakeer, Lubna Kamil Abdulhussein and Abdul Rahman, Mohd Fadhil and Yakasai, Mohd Hafeez and Abu Bakar, Nurlizah and Othman, Ahmad Razi and Syed, Mohd Arif and Abdullah, Norhani and Abd. Shukor, Mohd. Yunus (2017) Kinetic studies of the partially purified molybdenum-reducing enzyme from Bacillus pumilus strain Lbna. Bioremediation Science and Technology Research, 5 (1). pp. 18-23. ISSN 2289-5892 https://journal.hibiscuspublisher.com/index.php/BSTR/article/view/354
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
description Bacterial based remediation of environmental toxicants is a promising innovative technology for molybdenum pollution. To date, the enzyme responsible for molybdate reduction to Mo-blue from bacteria show that the Michaelis-Menten constants varies by one order of magnitude. It is important that the constants from newer enzyme sources be characterized so that a comparison can be made. The aim of this study is to characterize kinetically the enzyme from a previously isolated Mo-reducing bacterium; Bacillus pumilus strain Lbna. The maximum activity of this enzyme occurred at pH 5.5 and in between 25 and 35 °C. The Km and Vmax of NADH were 6.646 mM and 0.057 unit/mg enzyme, while the Km and Vmax of LPPM were 3.399 mM and 0.106 unit/mg enzyme. The results showed that the enzyme activity for Bacillus pumilus strain Lbna were inhibited by all heavy metals used. Zinc, copper, silver, chromium, cadmium and mercury all caused more than 50% inhibition to the Mo-reducing enzyme activity with copper being the most potent with an almost complete inhibition of enzyme activity observed.
format Article
author Abo-Shakeer, Lubna Kamil Abdulhussein
Abdul Rahman, Mohd Fadhil
Yakasai, Mohd Hafeez
Abu Bakar, Nurlizah
Othman, Ahmad Razi
Syed, Mohd Arif
Abdullah, Norhani
Abd. Shukor, Mohd. Yunus
spellingShingle Abo-Shakeer, Lubna Kamil Abdulhussein
Abdul Rahman, Mohd Fadhil
Yakasai, Mohd Hafeez
Abu Bakar, Nurlizah
Othman, Ahmad Razi
Syed, Mohd Arif
Abdullah, Norhani
Abd. Shukor, Mohd. Yunus
Kinetic studies of the partially purified molybdenum-reducing enzyme from Bacillus pumilus strain Lbna
author_facet Abo-Shakeer, Lubna Kamil Abdulhussein
Abdul Rahman, Mohd Fadhil
Yakasai, Mohd Hafeez
Abu Bakar, Nurlizah
Othman, Ahmad Razi
Syed, Mohd Arif
Abdullah, Norhani
Abd. Shukor, Mohd. Yunus
author_sort Abo-Shakeer, Lubna Kamil Abdulhussein
title Kinetic studies of the partially purified molybdenum-reducing enzyme from Bacillus pumilus strain Lbna
title_short Kinetic studies of the partially purified molybdenum-reducing enzyme from Bacillus pumilus strain Lbna
title_full Kinetic studies of the partially purified molybdenum-reducing enzyme from Bacillus pumilus strain Lbna
title_fullStr Kinetic studies of the partially purified molybdenum-reducing enzyme from Bacillus pumilus strain Lbna
title_full_unstemmed Kinetic studies of the partially purified molybdenum-reducing enzyme from Bacillus pumilus strain Lbna
title_sort kinetic studies of the partially purified molybdenum-reducing enzyme from bacillus pumilus strain lbna
publisher Hibiscus Publisher
publishDate 2017
url http://psasir.upm.edu.my/id/eprint/64017/1/Kinetic%20studies%20of%20the%20partially%20purified%20molybdenum-reducing%20enzyme%20from%20Bacillus%20pumilus%20strain%20Lbna.pdf
http://psasir.upm.edu.my/id/eprint/64017/
https://journal.hibiscuspublisher.com/index.php/BSTR/article/view/354
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score 13.160551