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dc.creatorde-la-Re-Vega,Enrique
dc.creatorGarcía-Orozco,Karina D
dc.creatorCalderón-Arredondo,Sergio A
dc.creatorRomo-Figueroa,María Gabriela
dc.creatorIslas-Osuna,María A.
dc.creatorYepiz-Plascencia,Gloria M.
dc.creatorSotelo-Mundo,Rogerio R.
dc.date2004-12-01
dc.date.accessioned2020-02-17T15:35:40Z
dc.date.available2020-02-17T15:35:40Z
dc.identifierhttps://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0717-34582004000300012
dc.identifier.urihttps://revistaschilenas.uchile.cl/handle/2250/132019
dc.descriptionShrimp Lysozyme (Lyz) is a key component of the antibacterial response as part of the innate defense in Crustacea; however, it has not been possible to purify this protein because of the very low amount present in the shrimp blood cells (hemocytes). In an effort to produce enough protein to study its function and biochemical properties we have overexpressed Lysozyme from marine shrimp (Penaeus vannamei) in E. coli. A bacterial protein expression system based on the T7 polymerase promoter was used. Although Lyz was produced as insoluble protein in inclusion bodies, its refolding led to an active protein with a yield of ~10%. Details of the protein recombinant expression techniques applied to this shrimp protein are presented
dc.formattext/html
dc.languageen
dc.publisherPontificia Universidad Católica de Valparaíso
dc.rightsinfo:eu-repo/semantics/openAccess
dc.sourceElectronic Journal of Biotechnology v.7 n.3 2004
dc.titleRecombinant expression of marine shrimp lysozyme in Escherichia coli


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