dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorLario, Luciana Daniela
dc.creatorChaud, Luciana
dc.creatorAlmeida, María das Graças
dc.creatorConverti, Attilio
dc.creatorDurães Sette, Lara
dc.creatorPessoa, Adalberto
dc.date2015-12-07T15:33:10Z
dc.date2016-10-25T21:23:06Z
dc.date2015-12-07T15:33:10Z
dc.date2016-10-25T21:23:06Z
dc.date2015
dc.date.accessioned2017-04-06T09:28:50Z
dc.date.available2017-04-06T09:28:50Z
dc.identifierFungal Biology, v. 119, n. 11, p. 1129-1136, 2015.
dc.identifier1878-6146
dc.identifierhttp://hdl.handle.net/11449/131262
dc.identifierhttp://acervodigital.unesp.br/handle/11449/131262
dc.identifier10.1016/j.funbio.2015.08.012
dc.identifier26466885
dc.identifierhttp://dx.doi.org/10.1016/j.funbio.2015.08.012
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/941802
dc.descriptionThe production, purification, and characterization of an extracellular protease released by Rhodotorula mucilaginosa L7 were evaluated in this study. This strain was isolated from an Antarctic marine alga and previously selected among others based on the capacity to produce the highest extracellular proteolytic activity in preliminary tests. R. mucilaginosa L7 was grown in Saboraud-dextrose medium at 25 °C, and the cell growth, pH of the medium, extracellular protease production and the glucose and protein consumption were determined as a function of time. The protease was then purified, and the effects of pH, temperature, and salt concentration on the catalytic activity and enzyme stability were determined. Enzyme production started at the beginning of the exponential phase of growth and reached a maximum after 48 h, which was accompanied by a decrease in the pH as well as reductions of the protein and glucose concentrations in the medium. The purified protease presented optimal catalytic activity at pH 5.0 and 50 °C. Finally, the enzyme was stable in the presence of high concentrations of NaCl. These characteristics are of interest for future studies and may lead to potential biotechnological applications that require enzyme activity and stability under acidic conditions and/or high salt concentrations.
dc.languageeng
dc.publisherElsevier B. V.
dc.relationFungal Biology
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectCold-adapted yeast
dc.subjectEnzyme characterization
dc.subjectExtracellular protease
dc.titleProduction, purification, and characterization of an extracellular acid protease from the marine Antarctic yeast Rhodotorula mucilaginosa L7
dc.typeOtro


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