Superior operational stability of immobilized l-asparaginase over surface-modified carbon nanotubes

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversity of Aveiro-
Autor(es): dc.contributorUniversity of Porto-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorAlmeida, Mafalda R.-
Autor(es): dc.creatorCristóvão, Raquel O.-
Autor(es): dc.creatorBarros, Maria A.-
Autor(es): dc.creatorNunes, João C. F.-
Autor(es): dc.creatorBoaventura, Rui A. R.-
Autor(es): dc.creatorLoureiro, José M.-
Autor(es): dc.creatorFaria, Joaquim L.-
Autor(es): dc.creatorNeves, Márcia C.-
Autor(es): dc.creatorFreire, Mara G.-
Autor(es): dc.creatorSantos-Ebinuma, Valéria C.-
Autor(es): dc.creatorTavares, Ana P. M.-
Autor(es): dc.creatorSilva, Cláudia G.-
Data de aceite: dc.date.accessioned2025-08-21T21:49:38Z-
Data de disponibilização: dc.date.available2025-08-21T21:49:38Z-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued2021-11-30-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1038/s41598-021-00841-2-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/222793-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/222793-
Descrição: dc.descriptionl-asparaginase (ASNase, EC 3.5.1.1) is an enzyme that catalyzes the l-asparagine hydrolysis into l-aspartic acid and ammonia, being mainly applied in pharmaceutical and food industries. However, some disadvantages are associated with its free form, such as the ASNase short half-life, which may be overcome by enzyme immobilization. In this work, the immobilization of ASNase by adsorption over pristine and modified multi-walled carbon nanotubes (MWCNTs) was investigated, the latter corresponding to functionalized MWCNTs through a hydrothermal oxidation treatment. Different operating conditions, including pH, contact time and ASNase/MWCNT mass ratio, as well as the operational stability of the immobilized ASNase, were evaluated. For comparison purposes, data regarding the ASNase immobilization with pristine MWCNT was detailed. The characterization of the ASNase-MWCNT bioconjugate was addressed using different techniques, namely Transmission Electron Microscopy (TEM), Thermogravimetric Analysis (TGA) and Raman spectroscopy. Functionalized MWCNTs showed promising results, with an immobilization yield and a relative recovered activity of commercial ASNase above 95% under the optimized adsorption conditions (pH 8, 60 min of contact and 1.5 × 10–3 g mL−1 of ASNase). The ASNase-MWCNT bioconjugate also showed improved enzyme operational stability (6 consecutive reaction cycles without activity loss), paving the way for its use in industrial processes.-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionFundação para a Ciência e a Tecnologia-
Descrição: dc.descriptionCICECO-Aveiro Institute of Materials Department of Chemistry University of Aveiro-
Descrição: dc.descriptionLaboratory of Separation and Reaction Engineering - Laboratory of Catalysis and Materials (LSRE-LCM) Department of Chemical Engineering Faculty of Engineering University of Porto, Rua do Dr. Roberto Frias-
Descrição: dc.descriptionDepartment of Engineering Bioprocess and Biotechnology School of Pharmaceutical Sciences São Paulo State University (Unesp)-
Descrição: dc.descriptionDepartment of Engineering Bioprocess and Biotechnology School of Pharmaceutical Sciences São Paulo State University (Unesp)-
Descrição: dc.descriptionFAPESP: 2018/06908-8-
Descrição: dc.descriptionFundação para a Ciência e a Tecnologia: POCI-01-0145-FEDER-031268-
Descrição: dc.descriptionFundação para a Ciência e a Tecnologia: UIDB/50011/2020-
Idioma: dc.languageen-
Relação: dc.relationScientific Reports-
???dc.source???: dc.sourceScopus-
Título: dc.titleSuperior operational stability of immobilized l-asparaginase over surface-modified carbon nanotubes-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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