Extracellular Expression of Keratinase from Bacillus licheniformis ER-15 in Escherichia coli
2010
Tiwary, Ekta | Gupta, Rani
Keratinase (ker BL) from Bacillus licheniformis ER-15 was cloned into vector pEZZ18 for extracellular expression in Escherichia coli HB101. Recombinant keratinase was secreted with high specific activity (75 units/mg) under non-inducible conditions after 36 h at 37 °C and 300 rpm in a shake flask. Protein was concentrated and, subsequently, purified by ion-exchange chromatography using Q-sepharose with 95.8% yield. The recombinant keratinase was a serine protease and most active in the pH range of 8−12 and at 60 °C. The enzyme was stable over a wide pH range of 4−12 for 3 h. ker BL degraded bovine serum albumin, casein, azocasein, gelatin, and feather. E. coli HB101 harboring pEZZ18 ker BL2 degraded chicken feather completely within 24 h at 37 °C.
Show more [+] Less [-]AGROVOC Keywords
Bibliographic information
This bibliographic record has been provided by National Agricultural Library