Secretory expression of thermostable T1 lipase through bacteriocin release protein

Abstract

The extracellular production of T1 lipase was performed by co-expression of pJL3 vector encoding bacteriocin release protein in prokaryotic system. Secretory expression was optimized by considering several parameters, including host strains, inducer (IPTG) concentration, media, induction at A 600 nm, temperature, and time of induction. Among the host strains tested, Origami B excreted out 18,100 U/ml of lipase activity into culture medium when induced with 50 μM IPTG for 12 h. The Origami B harboring recombinant plasmid pGEX/T1S and pJL3 vector was chosen for further study. IPTG at 0.05 mM, YT medium, induction at A600 nm of 1.25, 30°C, and 32 h of induction time were best condition for T1 lipase secretion with Origami B as a host. © 2005 Elsevier Inc. All rights reserved.