Improved L-Asparaginase Properties and Reusability by Immobilization onto Functionalized Carbon Xerogels

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversity of Porto-
Autor(es): dc.contributorCERES-
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.creatorCarneiro, Inês. G.-
Autor(es): dc.creatorBarros, Maria A.-
Autor(es): dc.creatorPereira, Matheus M.-
Autor(es): dc.creatorCarabineiro, Sónia A. 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.accessioned2025-08-21T18:19:35Z-
Data de disponibilização: dc.date.available2025-08-21T18:19:35Z-
Data de envio: dc.date.issued2025-04-29-
Data de envio: dc.date.issued2024-09-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1002/cplu.202400025-
Fonte completa do material: dc.identifierhttps://hdl.handle.net/11449/301661-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/301661-
Descrição: dc.descriptionEnzyme immobilization can offer a range of significant advantages, including reusability, and increased selectivity, stability, and activity. In this work, a central composite design (CCD) of experiments and response surface methodology (RSM) were used to study, for the first time, the L-asparaginase (ASNase) immobilization onto functionalized carbon xerogels (CXs). The best results were achieved using CXs obtained by hydrothermal oxidation with nitric acid and subsequent heat treatment in a nitrogen flow at 600 °C (CX−OX-600). Under the optimal conditions (81 min of contact time, pH 6.2 and 0.36 g/L of ASNase), an immobilization yield (IY) of 100 % and relative recovered activity (RRA) of 103 % were achieved. The kinetic parameters obtained also indicate a 1.25-fold increase in the affinity of ASNase towards the substrate after immobilization. Moreover, the immobilized enzyme retained 97 % of its initial activity after 6 consecutive reaction cycles. All these outcomes confirm the promising properties of functionalized CXs as support for ASNase, bringing new insights into the development of an efficient and stable immobilization platform for use in the pharmaceutical industry, food industry, and biosensors.-
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, Rua Dr. Roberto Frias-
Descrição: dc.descriptionALiCE – Associate Laboratory in Chemical Engineering Faculty of Engineering University of Porto, Rua Dr. Roberto Frias-
Descrição: dc.descriptionUniversity of Coimbra CERES Department of Chemical Engineering, Rua Sílvio Lima, Pólo II – Pinhal de Marrocos-
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.descriptionSão Paulo State University (UNESP) School of Pharmaceutical Sciences Department of Bioprocess Engineering and Biotechnology-
Descrição: dc.descriptionSão Paulo State University (UNESP) School of Pharmaceutical Sciences Department of Bioprocess Engineering and Biotechnology-
Descrição: dc.descriptionFundação para a Ciência e a Tecnologia: 2022.12055.BD-
Descrição: dc.descriptionFundação para a Ciência e a Tecnologia: SFRH/BD/145014/2019-
Idioma: dc.languageen-
Relação: dc.relationChemPlusChem-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectAdsorption-
Palavras-chave: dc.subjectBioconjugate-
Palavras-chave: dc.subjectFunctionalized carbon xerogels-
Palavras-chave: dc.subjectImmobilization-
Palavras-chave: dc.subjectL-asparaginase-
Título: dc.titleImproved L-Asparaginase Properties and Reusability by Immobilization onto Functionalized Carbon Xerogels-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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