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

Authors

  • Lubna Kamil Abdulhussein Abo-Shakeer Dept of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia.
  • Mohd Fadhil Abd Rahman Dept of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia.
  • Mohd Hafeez Yakasai Dept of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia.
  • Nurlizah Abu Bakar Institute of Ocean and Earth Sciences, Universiti Malaya, 50603 Kuala Lumpur, Malaysia.
  • Ahmad Razi Othman Department of Chemical Engineering and Process, Faculty of Engineering and Built Environment, Universiti Kebangsaan Malaysia (UKM), 43600 Bangi, Selangor, Malaysia.
  • Mohd Arif Syed Dept of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia.
  • Norhani Abdullah Institute of Tropical Agriculture and Food Security, Universiti Putra Malaysia 43400 UPM Serdang Selangor Darul Ehsan, Malaysia.
  • Mohd Yunus Shukor Dept of Biochemistry, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia.

DOI:

https://doi.org/10.54987/bstr.v5i1.354

Keywords:

molybdenum; Mo-reducing bacterium; Bacillus pumilus; Mo-reducing enzyme; Characterization;

Abstract

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 oC. 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.

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Published

2017-07-31

How to Cite

Abo-Shakeer, L. K. A., Rahman, M. F. A., Yakasai, M. H., Bakar, N. A., Othman, A. R., Syed, M. A., Abdullah, N., & Shukor, M. Y. (2017). Kinetic studies of the partially purified molybdenum-reducing enzyme from Bacillus pumilus strain lbna. Bioremediation Science and Technology Research (e-ISSN 2289-5892), 5(1), 18–23. https://doi.org/10.54987/bstr.v5i1.354

Issue

Vol. 5 No. 1 (2017)

Section

Articles

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