Immobilization and Characterization of L-Asparaginase over Carbon Xerogels

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversity of Porto-
Autor(es): dc.contributorUniversidade NOVA de Lisboa-
Autor(es): dc.contributorUniversity of Aveiro-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorBarros, Rita A. M.-
Autor(es): dc.creatorCristóvão, Raquel O.-
Autor(es): dc.creatorCarabineiro, Sónia A. C.-
Autor(es): dc.creatorNeves, Márcia C.-
Autor(es): dc.creatorFreire, Mara G.-
Autor(es): dc.creatorFaria, Joaquim L.-
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.accessioned2025-08-21T19:34:16Z-
Data de disponibilização: dc.date.available2025-08-21T19:34:16Z-
Data de envio: dc.date.issued2023-03-01-
Data de envio: dc.date.issued2023-03-01-
Data de envio: dc.date.issued2022-06-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.3390/biotech11020010-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/239961-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/239961-
Descrição: dc.descriptionL-asparaginase (ASNase) is an aminohydrolase currently used in the pharmaceutical and food industries. Enzyme immobilization is an exciting option for both applications, allowing for a more straightforward recovery and increased stability. High surface area and customizable porosity make carbon xerogels (CXs) promising materials for ASNase immobilization. This work describes the influence of contact time, pH, and ASNase concentration on the immobilization yield (IY) and relative recovered activity (RRA) using the Central Composite Design methodology. The most promising results were obtained using CX with an average pore size of 4 nm (CX-4), reaching IY and RRA of 100%. At the optimal conditions (contact time 49 min, pH 6.73, and [ASNase] 0.26 mg·mL−1), the ASNase-CXs biocomposite was characterized and evaluated in terms of kinetic properties and operational, thermal, and pH stabilities. The immobilized ASNase onto CX-4 retained 71% of its original activity after six continuous reaction cycles, showed good thermal stability at 37 °C (RRA of 91% after 90 min), and was able to adapt to both acidic and alkaline environments. Finally, the results indicated a 3.9-fold increase in the immobilized ASNase affinity for the substrate, confirming the potential of CXs as a support for ASNase and as a cost-effective tool for subsequent use in the therapeutic and food sectors.-
Descrição: dc.descriptionFederación Española de Enfermedades Raras-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionFundação para a Ciência e a Tecnologia-
Descrição: dc.descriptionLSRE-LCM—Laboratory of Separation and Reaction Engineering-Laboratory of Catalysis and Materials Faculty of Engineering University of Porto-
Descrição: dc.descriptionALiCE—Associate Laboratory in Chemical Engineering Faculty of Engineering University of Porto-
Descrição: dc.descriptionLAQV-REQUIMTE Department of Chemistry NOVA School of Science and Technology Universidade NOVA de Lisboa-
Descrição: dc.descriptionCICECO-Aveiro Institute of Materials Department of Chemistry University of Aveiro-
Descrição: dc.descriptionDepartment of Engineering Bioprocess and Biotechnology School of Pharmaceutical Sciences UNESP-University Estadual Paulista-
Descrição: dc.descriptionDepartment of Engineering Bioprocess and Biotechnology School of Pharmaceutical Sciences UNESP-University Estadual Paulista-
Descrição: dc.descriptionCNPq: 312463/2021-9-
Descrição: dc.descriptionFundação para a Ciência e a Tecnologia: CEECINST/00102/2018-
Idioma: dc.languageen-
Relação: dc.relationBioTech-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectcarbon xerogels-
Palavras-chave: dc.subjectcentral composite design-
Palavras-chave: dc.subjectenzyme immobilization-
Palavras-chave: dc.subjectL-asparaginase-
Palavras-chave: dc.subjectphysical adsorption-
Título: dc.titleImmobilization and Characterization of L-Asparaginase over Carbon Xerogels-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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