Stabilization of an amylase from Neurospora crassa by Immobilization on Highly Activated Supports

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dc.contributor.authorTavano, Olga L.
dc.contributor.authorPessela, Benevides C. C.
dc.contributor.authorGoulart, Antonio J.
dc.contributor.authorFernández-Lafuente, Roberto
dc.contributor.authorGuisán, José M.
dc.contributor.authorMonti, Rubens [UNESP]
dc.contributor.institutionInstituto de Quimica
dc.contributor.institutionInstituto de Fermentaciones Industriales-CSIC
dc.contributor.institutionSpain
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.contributor.institutionDepartamento de Biocatálisis
dc.date.accessioned2022-04-28T20:43:09Z
dc.date.available2022-04-28T20:43:09Z
dc.date.issued2008-01-01
dc.description.abstractThe amylase from Neurospora crassa is an interesting enzyme, having higher stability than amylase from Aspergillus oryzea under a broad range of pH values. Moreover, the N. crassa enzyme may be immobilized on different supports with good retention of enzyme activity. The best stabilizations were achieved using Eupergit C 250 L or glyoxyl agarose, with which the enzyme remained fully active at 60°C for 24 h while the soluble enzyme remained about 17%. The glyoxyl agarose immobilized enzyme had high thermostability, high optimal temperature (65°C) and broad pH/activity profile, suggesting that this enzyme has potential for food and industrial applications for starch modification. Copyright © Taylor & Francis Group, LLC.en
dc.description.affiliationDepartamento de Bioquimica e Tecnologia Quimica Instituto de Quimica, São Paulo
dc.description.affiliationDepartamento de Microbiologia de Alimentos Instituto de Fermentaciones Industriales-CSIC, Madrid
dc.description.affiliationDepartamento de Biocatálisis Instituto de Catálisis-CSIC Madrid Spain
dc.description.affiliationDepartamento de Alimentos e Nutrição, São Paulo
dc.description.affiliationDepartamento de Alimentos e Nutrição FCFUNESP, Rodovia Araraquara-Jaú Km 1, 14801 902, Araraquara, São Paulo
dc.description.affiliationInstituto de Catalisis Departamento de Biocatálisis Campus UAM, Cantoblanco. 28049 Madrid
dc.description.affiliationUnespDepartamento de Alimentos e Nutrição FCFUNESP, Rodovia Araraquara-Jaú Km 1, 14801 902, Araraquara, São Paulo
dc.format.extent262-275
dc.identifierhttp://dx.doi.org/10.1080/08905430802262616
dc.identifier.citationFood Biotechnology, v. 22, n. 3, p. 262-275, 2008.
dc.identifier.doi10.1080/08905430802262616
dc.identifier.issn1532-4249
dc.identifier.issn0890-5436
dc.identifier.scopus2-s2.0-49549092236
dc.identifier.urihttp://hdl.handle.net/11449/225248
dc.language.isoeng
dc.relation.ispartofFood Biotechnology
dc.sourceScopus
dc.subjectAmylase
dc.subjectEnzyme immobilization
dc.subjectEnzyme stabilization
dc.subjectGlyoxyl agarose
dc.subjectNeurospora crassa
dc.titleStabilization of an amylase from Neurospora crassa by Immobilization on Highly Activated Supportsen
dc.typeArtigo
unesp.departmentAlimentos e Nutrição - FCFpt

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Araraquara - FCF - Faculdade de Ciências Farmacêuticas