dc.creatorGonçalves, Thiago A.
dc.creatorSegato, Fernando
dc.creatorDamásio, André R. L.
dc.creatorLucas, Rosymar C. de
dc.creatorSquina, Fabio M.
dc.creatorDecker, Stephen R.
dc.creatorPrade, Rolf A.
dc.date2018-09-27T00:05:41Z
dc.date2018-09-27T00:05:41Z
dc.date2012-07-15
dc.date.accessioned2023-09-27T21:05:15Z
dc.date.available2023-09-27T21:05:15Z
dc.identifier0141-0229
dc.identifierhttps://doi.org/10.1016/j.enzmictec.2012.04.008
dc.identifierhttp://www.locus.ufv.br/handle/123456789/22016
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8954298
dc.descriptionProduction of pure and high-yield client proteins is an important technology that addresses the need for industrial applications of enzymes as well as scientific experiments in protein chemistry and crystallization. Fungi are utilized in industrial protein production because of their ability to secrete large quantities of proteins. In this study, we engineered a high-expression-secretion vector, pEXPYR that directs proteins towards the extracellular medium in two Aspergillii host strains, examine the effect of maltose-induced over-expression and protein secretion as well as time and pH-dependent protein stability in the medium. We describe five client proteins representing a core set of hemicellulose degrading enzymes that accumulated up to 50–100 mg/L of protein. Using a recyclable genetic marker that allows serial insertion of multiple genes, simultaneous hyper-secretion of three client proteins in a single host strain was accomplished.
dc.formatpdf
dc.formatapplication/pdf
dc.languageeng
dc.publisherEnzyme and Microbial Technology
dc.relationVolume 51, Issue 2, Pages 100-106, July 2012
dc.rightsElsevier B. V.
dc.subjectProtein production
dc.subjectProtein secretion
dc.subjectFungi
dc.subjectHeterologous expression and secretion of multiple proteins
dc.titleHigh-yield secretion of multiple client proteins in Aspergillus
dc.typeArtigo


Este ítem pertenece a la siguiente institución