dc.creatorRisso, FVA
dc.creatorMazutti, MA
dc.creatorCosta, F
dc.creatorTreichel, H
dc.creatorMaugeri, F
dc.creatorRodrigues, MI
dc.date2010
dc.dateOCT-DEC
dc.date2014-07-30T14:00:00Z
dc.date2015-11-26T17:41:49Z
dc.date2014-07-30T14:00:00Z
dc.date2015-11-26T17:41:49Z
dc.date.accessioned2018-03-29T00:23:38Z
dc.date.available2018-03-29T00:23:38Z
dc.identifierBrazilian Journal Of Chemical Engineering. Brazilian Soc Chemical Eng, v. 27, n. 4, n. 507, n. 516, 2010.
dc.identifier0104-6632
dc.identifierWOS:000286106200002
dc.identifier10.1590/S0104-66322010000400002
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/56144
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/56144
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1287119
dc.descriptionEnzymes have been extensively used in organic solvents to catalyze a variety of reactions of biological and industrial significance. In this work, the characteristics of free and immobilized inulinase were investigated in buffered solutions of butyl acetate. The influences of the organic solvent content on the optimal temperature and pH, the stabilities to temperature and pH and the kinetic parameters were systematically evaluated. The results showed that the organic solvent content had no effect on the optimal pH, either in the free or immobilized inulinase. For the immobilized enzyme, the optimal temperatures ranged from 55 degrees C to 60 degrees C, depending on the content of butyl acetate. At higher butyl acetate content, the stability of the immobilized enzyme increased for both pH and temperature. The organic solvent showed the tendency to increase the values of the kinetic parameters K-m and v(max) for both free and immobilized inulinase.
dc.description27
dc.description4
dc.description507
dc.description516
dc.languageen
dc.publisherBrazilian Soc Chemical Eng
dc.publisherSao Paulo
dc.publisherBrasil
dc.relationBrazilian Journal Of Chemical Engineering
dc.relationBraz. J. Chem. Eng.
dc.rightsaberto
dc.sourceWeb of Science
dc.subjectOrganic solvent
dc.subjectInulinase
dc.subjectStability
dc.subjectKinetic parameters
dc.subjectSucrose Hydrolysis
dc.subjectEnzymes
dc.subjectSolvents
dc.subjectLipase
dc.titleCOMPARATIVE STUDIES OF THE STABILITY OF FREE AND IMMOBILIZED INULINASE FROM Kluyveromyces marxianus NRRL Y-7571 IN AQUEOUS-ORGANIC SOLUTIONS
dc.typeArtículos de revistas


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