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Partitioning of the glucoamylase activity at the cell surfaces in cultures of Saccharomyces

dc.contributor.authorPeres, MFS
dc.contributor.authorSouza, C. S.
dc.contributor.authorThomaz, D.
dc.contributor.authorde Souza, A. R.
dc.contributor.authorLaluce, Cecília [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2014-05-20T15:24:30Z
dc.date.available2014-05-20T15:24:30Z
dc.date.issued2006-01-01
dc.description.abstractGlucoamylases have been used with alpha-amylases for the industrial conversion of starch into glucose. However, little is known about the properties of this glycosylated protein retained in the cell wall of Saccharomyces as well as its role in the saccharification and fermentation of amylaceous substrates, notably in high cell density processes. In most of the strains assayed, decreases in biomass formation were followed by increases in glucoamylase secretion (expressed as U/mg(biomass) in 1 ml of culture) when glucose was exchanged for starch as carbon source or the growth temperature was raised from 30 to 35 degrees C. Despite the losses in viability, significant increases in the activity of the wall fraction occurred when cultures of thermotolerant yeasts propagated at 30 degrees C or washed cells resuspended in buffer solution were heated to 60 degrees C for 60-80 min prior to amylolytic assays. Thus, intact cells of thermotolerant yeasts can be used as colloidal biocatalysts in starch degradation processes. (C) 2005 Published by Elsevier Ltd.en
dc.description.affiliationUNESP, Inst Quim, Dept Bioquim & Tecnol Quim, BR-14801970 Araraquara, SP, Brazil
dc.description.affiliationFac Filosofia Ciências & Letras Ribeirao Pret, Program Posgrad Quim, Ribeirao Preto, Brazil
dc.description.affiliationUSP, BUTATAN, IPT, Programa Posgrad Interunidades Biotecnol, São Paulo, Brazil
dc.description.affiliationUSP S Carlos, Inst Quim, Programa Posgrad Quim, Sao Carlos, SP, Brazil
dc.description.affiliationUnespUNESP, Inst Quim, Dept Bioquim & Tecnol Quim, BR-14801970 Araraquara, SP, Brazil
dc.format.extent20-27
dc.identifierhttp://dx.doi.org/10.1016/j.procbio.2005.01.027
dc.identifier.citationProcess Biochemistry. Oxford: Elsevier B.V., v. 41, n. 1, p. 20-27, 2006.
dc.identifier.dimensionspub.1003617009
dc.identifier.doi10.1016/j.procbio.2005.01.027
dc.identifier.issn1359-5113
dc.identifier.issn1873-3298
dc.identifier.orcid0000-0001-7149-5993
dc.identifier.orcid0000-0002-2462-7997
dc.identifier.urihttp://hdl.handle.net/11449/35102
dc.identifier.wosWOS:000234658500003
dc.language.isoeng
dc.publisherElsevier B.V.
dc.publisherElsevier
dc.relation.ispartofProcess Biochemistry
dc.relation.ispartofjcr2.616
dc.relation.ispartofsjr0,761
dc.rights.accessRightsAcesso restritopt
dc.sourceWeb of Science
dc.sourceDimensions
dc.subjectyeastpt
dc.subjectSaccharomycespt
dc.subjectglucoamylase secretionpt
dc.subjectamylolytic enzymespt
dc.subjectthermal stabilitypt
dc.subjectcell-wall glucoamylasept
dc.titlePartitioning of the glucoamylase activity at the cell surfaces in cultures of Saccharomycesen
dc.typeArtigopt
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
dspace.entity.typePublication
relation.isOrgUnitOfPublicationbc74a1ce-4c4c-4dad-8378-83962d76c4fd
relation.isOrgUnitOfPublication.latestForDiscoverybc74a1ce-4c4c-4dad-8378-83962d76c4fd
unesp.author.lattes6423374942748412[5]
unesp.author.orcid0000-0002-2462-7997[5]
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Química, Araraquarapt
unesp.departmentBioquímica e Tecnologia - IQpt

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