dc.creatorObregon, Walter David
dc.creatorCisneros, José Sebastián
dc.creatorCeccacci, Florencia
dc.creatorQuiroga, Evelina
dc.date.accessioned2016-05-16T14:49:48Z
dc.date.accessioned2018-11-06T15:30:51Z
dc.date.available2016-05-16T14:49:48Z
dc.date.available2018-11-06T15:30:51Z
dc.date.created2016-05-16T14:49:48Z
dc.date.issued2015-05
dc.identifierObregon, Walter David; Cisneros, José Sebastián; Ceccacci, Florencia; Quiroga, Evelina; A highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease; OMICS; Journal of Bioprocessing & Biotechniques; 5; 3; 5-2015; 1000211-1000211
dc.identifier2155-9821
dc.identifierhttp://hdl.handle.net/11336/5680
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1897981
dc.description.abstractIn this work, araujiain (enzymatic preparation obtained from the latex of Araujia hortorum fruits) was successfully immobilized on glyoxyl-agarose via multipoint covalent attachment. Thus, good efficiency of immobilization and high operational stability of immobilized enzyme were obtained. The activity of araujiain at alkaline pH was significantly improved after immobilization. In addition, immobilized araujiain also showed high activity and good stability, without significant loss in its activity, at temperatures between 37 and 60°C and in the presence of immiscible organic solvents. Immobilized araujiain also showed good performance in a mixture of 50% ethyl acetate in buffer, used for peptide synthesis, with better results than when the free enzyme was used as catalyst. These results indicate that immobilized araujiain via multipoint covalent attachment can be highly stabilized and this method might be used for practical applications of araujiain in hydrolytic and synthetic processes.
dc.languageeng
dc.publisherOMICS
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://goo.gl/uwtLDh
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.4172/2155-9821.1000211
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/10.4172/2155-9821.1000211
dc.rightshttps://creativecommons.org/licenses/by/2.5/ar/
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectARAUJIAIN
dc.subjectPROTEASE
dc.subjectENZYME
dc.subjectIMMOBILIZED
dc.titleA highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease
dc.typeArtículos de revistas
dc.typeArtículos de revistas
dc.typeArtículos de revistas


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