Secretory expression of thermostable T1 lipase through bacteriocin release protein

Raja Abdul Rahman, Raja Noor Zaliha and Thean, Chor Leow and Basri, Mahiran and Salleh, Abu Bakar (2005) Secretory expression of thermostable T1 lipase through bacteriocin release protein. Protein Expression and Purification, 40 (2). pp. 411-416. ISSN 1046-5928

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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 A600 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.

Item Type:Article
Keyword:Geobacillus sp., Thermostable lipase, GST fusion protein, Bacteriocin release protein
Faculty or Institute:Faculty of Science
Publisher:Elsevier Inc.
DOI Number:10.1016/j.pep.2005.01.006
ID Code:7073
Deposited By: Erni Suraya Abdul Aziz
Deposited On:04 Jun 2010 08:25
Last Modified:04 Jun 2010 08:27

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