High stabilization and hyperactivation of a recombinant β-Xylosidase through immobilization strategies

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dc.contributorLEDV - Laboratório de Desenvolvimento de Vacinaspt_BR
dc.contributor.authorCorradini, Felipe A.S.pt_BR
dc.contributor.authorMilessi, Thais S.pt_BR
dc.contributor.authorGonçalves, Viviane Maimonipt_BR
dc.contributor.authorRuller, Robertopt_BR
dc.contributor.authorSargo, Cíntia R.pt_BR
dc.contributor.authorLopes, Laiane A.pt_BR
dc.contributor.authorZangirolami, Teresa C.pt_BR
dc.contributor.authorTardioli, Paulo W.pt_BR
dc.contributor.authorGiordano, Roberto C.pt_BR
dc.contributor.authorGiordano, Raquel L.C.pt_BR
dc.date.accessioned2021-02-05T14:02:00Z-
dc.date.available2021-02-05T14:02:00Z-
dc.date.issued2021pt_BR
dc.identifier.citationCorradini FA.S., Milessi TS., Gonçalves VM, Ruller R, Sargo CR., Lopes LA., et al. High stabilization and hyperactivation of a recombinant β-Xylosidase through immobilization strategies. Enzyme Microb Technol. 2021 Apr;145:109725. doi:10.1016/j.enzmictec.2020.109725.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/3513-
dc.description.abstractAttainment of a stable and highly active β-xylosidase is of major importance for the efficient and cost-competitive hydrolysis of hemicellulose xylan, as well as for its industrial conversion into biofuels and biochemicals. Here, a recombinant β-xylosidase of the glycoside hydrolase family (GH43) from Bacillus subtilis was produced in Escherichia coli culture, purified, and subsequently immobilized on agarose and chitosan. Glutaraldehyde and glyoxyl groups were evaluated as activating agents to select the most efficient derivative. Multi-point immobilization on agarose led to an extraordinary thermal stability (half-lives 3604 and 164-fold higher than the free enzyme, at 50° and 35 °C, respectively). Even for chitosan activated with glutaraldehyde, a low-cost support, thermal stability of the immobilized enzyme was 326 and 12-fold higher than the free enzyme at 50° and 35°C, respectively. Immobilized enzymes showed no release of any subunit for the agarose-glyoxyl derivative, and only a few ones for the support activated with glutaraldehyde. Most remarkably, the enzyme kinetic behavior after immobilization increased up to 4-fold in relation to the free one. β-xylosidase, a tetrameric enzyme with four identical subunits, exists in equilibrium between the monomeric and oligomeric forms in solution. Depending on the pH of immobilization, the enzyme oligomerization can be favored, thus explaining the hyperactivation phenomenon. Both glyoxyl-agarose and chitosan-glutaraldehyde derivatives were used to catalyze corncob xylan hydrolysis, reaching 72 % conversion, representing a xylose productivity of around 20 g L−1 h−1. After ten 4h-cycles (pH 6.0, 35 °C), the xylan-to-xylose conversion remained approximately unchanged. Therefore, the immobilized β-xylosidases prepared in this work can be of great interest as biocatalysts in a biorefinery context.pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)pt_BR
dc.format.extent109725pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofEnzyme and Microbial Technologypt_BR
dc.rightsOpen Accesspt_BR
dc.titleHigh stabilization and hyperactivation of a recombinant β-Xylosidase through immobilization strategiespt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1016/j.enzmictec.2020.109725pt_BR
dc.identifier.urlhttps://doi.org/10.1016/j.enzmictec.2020.109725pt_BR
dc.contributor.externalUniversidade Federal de São Carlos (UFSCar)pt_BR
dc.contributor.externalUniversidade Federal de Itajubá (UNIFEI)pt_BR
dc.contributor.externalUniversidade Federal de Mato Grosso do Sul (UFMS)pt_BR
dc.contributor.externalCentro Nacional de Pesquisa em Energia e Materiais (CNPEM)pt_BR
dc.identifier.citationvolume145pt_BR
dc.subject.keywordEnzyme stabilizationpt_BR
dc.subject.keywordβ-xylosidasept_BR
dc.subject.keywordXylan hydrolysispt_BR
dc.subject.keywordHemicellulose hydrolysispt_BR
dc.subject.keywordEnzyme immobilizationpt_BR
dc.relation.ispartofabbreviatedEnzyme Microb Technolpt_BR
dc.identifier.citationabntv. 145, 109725, abr. 2021pt_BR
dc.identifier.citationvancouver2021 Apr;145:109725pt_BR
dc.contributor.butantanGonçalves, Viviane Maimoni|:Pesquisador|:Laboratório de Desenvolvimento de Vacinas (LEDV)pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦146438/2015-9pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦429829/2016-7pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2016/10.636-8pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2018/06696-0pt_BR
dc.sponsorship.butantanCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)¦¦001pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
item.grantfulltextembargo_29990101-
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