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Purification of dibenzothiophene monooxygenase from a recombinant Escherichia coli
- Gupta, Nidhi, Adhikari, D. K., Stobdan, T., Roychoudhury, P. K., Deb, J. K.
- Biotechnology letters 2007 v.29 no.10 pp. 1465-1468
- Escherichia coli, affinity chromatography, gene expression
- 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.