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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| Format: | Article |
| Language: | English |
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Hibiscus Publisher
2017
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| Online Access: | http://psasir.upm.edu.my/id/eprint/64017/ http://psasir.upm.edu.my/id/eprint/64017/1/Kinetic%20studies%20of%20the%20partially%20purified%20molybdenum-reducing%20enzyme%20from%20Bacillus%20pumilus%20strain%20Lbna.pdf |
| _version_ | 1848854886216630272 |
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| 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 |
| 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 |
| building | UPM Institutional Repository |
| collection | Online Access |
| 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. |
| first_indexed | 2025-11-15T11:16:59Z |
| format | Article |
| id | upm-64017 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T11:16:59Z |
| publishDate | 2017 |
| publisher | Hibiscus Publisher |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-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 |
| 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 |
| title | 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_short | 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 |
| url | http://psasir.upm.edu.my/id/eprint/64017/ http://psasir.upm.edu.my/id/eprint/64017/ http://psasir.upm.edu.my/id/eprint/64017/1/Kinetic%20studies%20of%20the%20partially%20purified%20molybdenum-reducing%20enzyme%20from%20Bacillus%20pumilus%20strain%20Lbna.pdf |