Show simple item record

dc.contributor.authorGiraldo, Marielle Aleixo [UNESP]
dc.contributor.authorGoncalves, Heloisa Bressan [UNESP]
dc.contributor.authorMelo Furriel, Rosa dos Prazeres
dc.contributor.authorJorge, Joo Atilio
dc.contributor.authorSouza Guimares, Luis Henrique
dc.date.accessioned2014-12-03T13:08:52Z
dc.date.available2014-12-03T13:08:52Z
dc.date.issued2014-05-01
dc.identifierhttp://dx.doi.org/10.1007/s11274-013-1570-3
dc.identifier.citationWorld Journal Of Microbiology & Biotechnology. New York: Springer, v. 30, n. 5, p. 1501-1510, 2014.
dc.identifier.issn0959-3993
dc.identifier.urihttp://hdl.handle.net/11449/111667
dc.description.abstractThe filamentous fungus Aspergillus terreus secretes both invertase and beta-glucosidase when grown under submerged fermentation containing rye flour as the carbon source. The aim of this study was to characterize the co-purified fraction, especially the invertase activity. An invertase and a beta-glucosidase were co-purified by two chromatographic steps, and the isolated enzymatic fraction was 139-fold enriched in invertase activity. SDS-PAGE analysis of the co-purified enzymes suggests that the protein fraction with invertase activity was heterodimeric, with subunits of 47 and 27 kDa. Maximal invertase activity, which was determined by response surface methodology, occurred in pH and temperature ranges of 4.0-6.0 and 55-65 A degrees C, respectively. The invertase in co-purified enzymes was stable for 1 h at pH 3.0-10.0 and maintained full activity for up to 1 h at 55 A degrees C when diluted in water. Invertase activity was stimulated by 1 mM concentrations of Mn2+ (161 %), Co2+ (68 %) and Mg2+ (61 %) and was inhibited by Al3+, Ag+, Fe2+ and Fe3+. In addition to sucrose, the co-purified enzymes hydrolyzed cellobiose, inulin and raffinose, and the apparent affinities for sucrose and cellobiose were quite similar (K-M = 22 mM). However, in the presence of Mn2+, the apparent affinity and V-max for sucrose hydrolysis increased approximately 2- and 2.9-fold, respectively, while for cellobiose, a 2.6-fold increase in V-max was observed, but the apparent affinity decreased 5.5-fold. Thus, it is possible to propose an application of this multifunctional extract containing both invertase and beta-glucosidase to degrade plant biomass, thus increasing the concentration of monosaccharides obtained from sucrose and cellobiose.en
dc.format.extent1501-1510
dc.language.isoeng
dc.publisherSpringer
dc.relation.ispartofWorld Journal of Microbiology & Biotechnology
dc.sourceWeb of Science
dc.subjectInvertaseen
dc.subjectAspergillusen
dc.subjectbeta-glucosidaseen
dc.subjectFructofuranosidaseen
dc.subjectMultifunctional extracten
dc.titleCharacterization of the co-purified invertase and beta-glucosidase of a multifunctional extract from Aspergillus terreusen
dc.typeArtigo
dcterms.licensehttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dcterms.rightsHolderSpringer
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.description.affiliationUNESP, Inst Quim Araraquara, BR-14800900 Araraquara, SP, Brazil
dc.description.affiliationUniv Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, BR-14040901 Ribeirao Preto, SP, Brazil
dc.description.affiliationUnespUNESP, Inst Quim Araraquara, BR-14800900 Araraquara, SP, Brazil
dc.identifier.doi10.1007/s11274-013-1570-3
dc.identifier.wosWOS:000333620600007
dc.rights.accessRightsAcesso restrito
unesp.author.orcid0000-0002-2921-3929[5]
unesp.author.orcid0000-0003-3882-362X[3]
dc.relation.ispartofjcr2.100
dc.relation.ispartofsjr0,604
Localize o texto completo

Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record