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1 mai 2011
- handle: 10670/1.cb6ihc
info:eu-repo/semantics/openAccess
Mots-clés
antibacterial activity inclusion body lysozyme on-column refolding recombinant expression Spodoptera lituraSujets proches
Muramidase Mucopeptide glucohydrolaseCiter ce document
Jong-Wan Kim et al., « Recombinant expression and refolding of the c-type lysozyme from Spodoptera litura in E. coli », Electronic Journal of Biotechnology, ID : 10670/1.cb6ihc
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Résumé
The chicken-type lysozyme of the insect Spodoptera litura (SLLyz) is a polypeptide of 121 amino acids containing four disulfide bridges and 17 rare codons and participates in innate defense as an anti-bacterial enzyme. The recombinant S. litura lysozyme (rSLLyz) expressed as a C-terminal fusion protein with glutathione S-transferase (GST) in Rosetta(DE3) Singles. The protein was produced as an inclusion body which was solubilized in 8 M urea, renatured by on-column refolding, and purified by reversed-phase chromatography to 95% purity. The purified rSLLyz demonstrated antibacterial activity against B. megaterium confirmed by inhibition zone assay. The overexpression and refolding strategy described in this study will provide a reliable technique for maximizing production and purification of proteins expressed as inclusion bodies in E. coli.