Purification of dibenzothiophene monooxygenase from a recombinant Escherichia coli.
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.
Gupta
Nidhi
N
Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology, Delhi, Hauz Khas, New Delhi, 110016, India.
Adhikari
D K
DK
Stobdan
T
T
Roychoudhury
P K
PK
Deb
J K
JK
D000595:Amino Acid Sequence; D001483:Base Sequence; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics*; D005822:Genetic Vectors / Q000235:genetics; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D011994:Recombinant Proteins / Q000302:isolation & purification* / Q000378:metabolism; D016415:Sequence Alignment; D013696:Temperature; D013876:Thiophenes / Q000378:metabolism
D011994:Recombinant Proteins; D013876:Thiophenes; D010088:Oxidoreductases; C090100:dibenzothiophene monooxygenase; C016366:dibenzothiophene