Functional expression of an alkaline lipase inEscherichia coli

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• 作者：Mohammed Rabbani (1)
  Hamid Mirmohammadsadeghi (1)
  Mohsen Ani (2)
  Koorosh Goodarzvand Chegini (2)
  Zahra Etemadifar (3)
  Fatemeh Moazen (1)
  
• 关键词：alkaline lipase ; Escherichia coli BL21(DE3) ; pET15b ; ZnCl2
• 刊名：Annals of Microbiology
• 出版年：2009
• 出版时间：December 2009
• 年：2009
• 卷：59
• 期：4
• 页码：763-769
• 全文大小：387KB
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• 作者单位：Mohammed Rabbani (1)
  Hamid Mirmohammadsadeghi (1)
  Mohsen Ani (2)
  Koorosh Goodarzvand Chegini (2)
  Zahra Etemadifar (3)
  Fatemeh Moazen (1)
  
  1. Department of Pharmaceutical Biotechnology, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
  2. Department of Clinical Biochemistry and Isfahan Pharmaceutical Sciences Research Center, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Isfahan, Iran
  3. Department of Biology, School of Basic Sciences, University of Isfahan, Isfahan, Iran
  
• ISSN：1869-2044

文摘

The aim of the present study was to express and evaluate a previously cloned lipase gene. In this study, the cloned gene was subcloned in the pET15bEscherichia coli BL21(DE3) expression system. The expression of the recombinant lipase was induced using 1 mM IPTG for 3 hours. The enzyme activity was measured using p-nitrophenyl-decanoate as substrate. The recombinant lipase showed a molecular weight of 26 kDa by SDS-PAGE. Maximum activity was found at pH 9-10 and 40-50 °C. ZnCl2 at 1, 0.3, 0.1, 0.03, and 0.01 mM concentrations were found to be inhibitory to the enzyme activity and did not improve enzyme thermostability. The recombinant lipase showed an optimum temperature higher than lipase ofBacillus subtilis (its closest relative in primary structure) while similar activity in the alkaline pH.