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Purification of dibenzothiophene monooxygenase from a recombinant Escherichia coli

Author:
Gupta, Nidhi, Adhikari, D. K., Stobdan, T., Roychoudhury, P. K., Deb, J. K.
Source:
Biotechnology letters 2007 v.29 no.10 pp. 1465-1468
ISSN:
0141-5492
Subject:
Escherichia coli, affinity chromatography, gene expression
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.
Agid:
2751071