Show simple item record

dc.creatorKim,Jong-Wan
dc.creatorYoe,Jeehyun
dc.creatorLee,Gil Ho
dc.creatorYoe,Sung Moon
dc.date2011-05-01
dc.date.accessioned2019-05-03T12:44:50Z
dc.date.available2019-05-03T12:44:50Z
dc.identifierhttps://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0717-34582011000300006
dc.identifier.urihttp://revistaschilenas.uchile.cl/handle/2250/85206
dc.descriptionThe 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.
dc.formattext/html
dc.languageen
dc.publisherPontificia Universidad Católica de Valparaíso
dc.rightsinfo:eu-repo/semantics/openAccess
dc.sourceElectronic Journal of Biotechnology v.14 n.3 2011
dc.subjectantibacterial activity
dc.subjectinclusion body
dc.subjectlysozyme
dc.subjecton-column refolding
dc.subjectrecombinant expression
dc.subjectSpodoptera litura
dc.titleRecombinant expression and refolding of the c-type lysozyme from Spodoptera litura in E. coli


This item appears in the following Collection(s)

Show simple item record