Abstract
Dibenzothiophene monooxygenase is the first enzyme involved in the degradation of dibenzothiophene. This gene was expressed via the pET28a vector in E. coli and was purified in a single step using affinity chromatography. The protein was purified 39-fold with a specific activity of 38 U/mg.
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Acknowledgements
We would like to thank Centre for High Technology, Oil India Development Board, Government of India, for the generous financial support (JKD and PKRC) and Council of Scientific and Industrial Research, Government of India for providing research fellowship (NG).
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Gupta, N., Adhikari, D.K., Stobdan, T. et al. Purification of dibenzothiophene monooxygenase from a recombinant Escherichia coli . Biotechnol Lett 29, 1465–1468 (2007). https://doi.org/10.1007/s10529-007-9431-5
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DOI: https://doi.org/10.1007/s10529-007-9431-5