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dc.contributor.CRUESPUNIVERSIDADE DE ESTADUAL DE CAMPINASpt_BR
dc.typeArtigo de periódicopt_BR
dc.titleEffects Of High Pressure Homogenization On The Activity, Stability, Kinetics And Three-dimensional Conformation Of A Glucose Oxidase Produced By Aspergillus Nigerpt_BR
dc.contributor.authorTribst A.A.L.pt_BR
dc.contributor.authorCota J.pt_BR
dc.contributor.authorMurakami M.T.pt_BR
dc.contributor.authorCristianini M.pt_BR
unicamp.authorTribst, A.A.L., Department of Food Technology (DTA), School of Food Engineering (FEA), University of Campinas (UNICAMP), Campinas, SP, Brazilpt_BR
unicamp.authorCota, J., Department of Food Science (DCA), School of Food Engineering (FEA), University of Campinas (UNICAMP), Campinas, SP, Brazil, Brazilian Bioethanol Science and Technology Laboratory (CTBE/CNPEM), Campinas, SP, Brazilpt_BR
unicamp.authorCristianini, M., Department of Food Technology (DTA), School of Food Engineering (FEA), University of Campinas (UNICAMP), Campinas, SP, Brazilpt_BR
unicamp.author.externalMurakami, M.T., Brazilian Biosciences National Laboratory (LNBio/CNPEM), Campinas, SP, Brazilpt
dc.description.abstractHigh pressure homogenization (HPH) is a non-thermal method, which has been employed to change the activity and stability of biotechnologically relevant enzymes. This work investigated how HPH affects the structural and functional characteristics of a glucose oxidase (GO) from Aspergillus niger. The enzyme was homogenized at 75 and 150 MPa and the effects were evaluated with respect to the enzyme activity, stability, kinetic parameters and molecular structure. The enzyme showed a pH-dependent response to the HPH treatment, with reduction or maintenance of activity at pH 4.5-6.0 and a remarkable activity increase (30-300%) at pH 6.5 in all tested temperatures (15, 50 and 75°C). The enzyme thermal tolerance was reduced due to HPH treatment and the storage for 24 h at high temperatures (50 and 75°C) also caused a reduction of activity. Interestingly, at lower temperatures (15°C) the activity levels were slightly higher than that observed for native enzyme or at least maintained. These effects of HPH treatment on function and stability of GO were further investigated by spectroscopic methods. Both fluorescence and circular dichroism revealed conformational changes in the molecular structure of the enzyme that might be associated with the distinct functional and stability behavior of GO. © 2014 Tribst et al.en
dc.relation.ispartofPLoS ONEpt_BR
dc.publisherPublic Library of Sciencept_BR
dc.date.issued2014pt_BR
dc.identifier.citationPlos One. Public Library Of Science, v. 9, n. 7, p. - , 2014.pt_BR
dc.language.isoenpt_BR
dc.description.volume9pt_BR
dc.description.issuenumber7pt_BR
dc.rightsabertopt_BR
dc.sourceScopuspt_BR
dc.identifier.issn19326203pt_BR
dc.identifier.doi10.1371/journal.pone.0103410pt_BR
dc.identifier.urlhttp://www.scopus.com/inward/record.url?eid=2-s2.0-84904910904&partnerID=40&md5=d1132cb48b6233b9c00b48c21c05c95cpt_BR
dc.date.available2015-06-25T17:55:15Z
dc.date.available2015-11-26T14:36:37Z-
dc.date.accessioned2015-06-25T17:55:15Z
dc.date.accessioned2015-11-26T14:36:37Z-
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dc.description.provenanceMade available in DSpace on 2015-11-26T14:36:37Z (GMT). No. of bitstreams: 2 2-s2.0-84904910904.pdf: 1386950 bytes, checksum: de31fc72184246131f03f090b9da613f (MD5) 2-s2.0-84904910904.pdf.txt: 35796 bytes, checksum: 6079d50de214d621be6def4befcba3e6 (MD5) Previous issue date: 2014en
dc.identifier.urihttp://www.repositorio.unicamp.br/handle/REPOSIP/86789
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/86789-
dc.identifier.idScopus2-s2.0-84904910904pt_BR
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