Purification of dibenzothiophene monooxygenase from a recombinant Escherichia coli
IR@IIP: CSIR-Indian Institute of Petroleum, Dehradun
View Archive Info| Field | Value | |
| Creator |
Gupta,Nidhi
Adhikari,D.K Stobdan,Tsering Roychoudhury,P.K Deb,J.K |
|
| Date |
2009-06-22T10:39:40Z
2009-06-22T10:39:40Z 2009-06-22T10:39:40Z |
|
| Identifier |
http://hdl.handle.net/123456789/234
|
|
| Description |
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.
Keywords Affinity chromatography,
Biodesulfurization,Dibenzothiophene,
Monooxygenase,Rhodococcus
|
|
| Language |
en_US
|
|
| Subject |
Affinity chromatography
Biodesulfurization Dibenzothiophene Monooxygenase Rhodococcus |
|
| Title |
Purification of dibenzothiophene monooxygenase from a recombinant Escherichia coli
|
|
| Type |
Article
|
|