dc.creatorBalsan, G
dc.creatorAstolfi, V
dc.creatorBenazzi, T
dc.creatorMeireles, MAA
dc.creatorMaugeri, F
dc.creatorDi Luccio, M
dc.creatorDal Pra, V
dc.creatorMossi, AJ
dc.creatorTreichel, H
dc.creatorMazutti, MA
dc.date2012
dc.dateSEP
dc.date2014-07-30T16:51:50Z
dc.date2015-11-26T16:35:05Z
dc.date2014-07-30T16:51:50Z
dc.date2015-11-26T16:35:05Z
dc.date.accessioned2018-03-28T23:17:28Z
dc.date.available2018-03-28T23:17:28Z
dc.identifierBioprocess And Biosystems Engineering. Springer, v. 35, n. 7, n. 1229, n. 1237, 2012.
dc.identifier1615-7591
dc.identifierWOS:000307514500020
dc.identifier10.1007/s00449-012-0710-8
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/62795
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/62795
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1271400
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionThis work is focused on the characterization of a commercial cellulase in terms of optimum pH and temperature, stability to pH and temperature and affinity of this enzyme to several substrates, determining the Michaelis-Menten parameters. Maximum activity of cellulase was obtained for the temperature range from 40 to 50 A degrees C and pH from 5.2 to 5.5. Enzyme activity decreased only 15% after 150 h of reaction at temperatures between 30 and 50 A degrees C. No loss of activity was observed at pH 5.0 and 5.5. The cellulase showed satisfactory results in the hydrolysis of agroindustrial substrates, since similar activity was verified on filter paper and other agroindustrial substrates.
dc.description35
dc.description7
dc.description1229
dc.description1237
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFapergs
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.languageen
dc.publisherSpringer
dc.publisherNew York
dc.publisherEUA
dc.relationBioprocess And Biosystems Engineering
dc.relationBioprocess. Biosyst. Eng.
dc.rightsfechado
dc.rightshttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dc.sourceWeb of Science
dc.subjectCellulase
dc.subjectAgroindustrial substrates
dc.subjectEnzymatic hydrolysis
dc.subjectLignocellulosic
dc.subjectThermal Inactivation
dc.subjectEnzymatic-hydrolysis
dc.subjectTomato Juice
dc.subjectSolid-state
dc.subjectFermentation
dc.subjectPurification
dc.subjectEnzymes
dc.subjectDeactivation
dc.subjectTechnologies
dc.subjectPretreatment
dc.titleCharacterization of a commercial cellulase for hydrolysis of agroindustrial substrates
dc.typeArtículos de revistas


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