Nanozeolites as support for laccase immobilization: Application to mediated glycerol oxidation

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorJames Parsons Building-
Autor(es): dc.creatorMiller, Alex Henrique-
Autor(es): dc.creatorde Vasconcellos, Adriano-
Autor(es): dc.creatorFielding, Alistair John-
Autor(es): dc.creatorNery, José Geraldo-
Data de aceite: dc.date.accessioned2025-08-21T18:08:01Z-
Data de disponibilização: dc.date.available2025-08-21T18:08:01Z-
Data de envio: dc.date.issued2022-04-29-
Data de envio: dc.date.issued2022-04-29-
Data de envio: dc.date.issued2021-09-25-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.apcata.2021.118361-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/229609-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/229609-
Descrição: dc.descriptionThis study investigated the use of nanozeolites as support for laccases from P. ostreatus (LPO), Aspergillus sp (LAsp) and A. bisporus (LAB) immobilization applied to 2,2,6,6-tetramethylpiperidine-N-oxyl (TEMPO) mediated glycerol oxidation. Selected complexes led to up to 5% glycerol conversion, and interestingly, up to 100% selectivity to glyceraldehyde after 48 h. Free enzymes led to significantly higher yields (up to 82%) but lacked selectivity when tested under the same conditions. These findings suggest that laccases immobilized into nanozeolites are promising catalysts for the selective oxidation of glycerol. With the aim to understand the different behavior of free or immobilized enzymes, electron paramagnetic resonance (EPR) spectroscopy was applied. A significant shift of the T2 parallel copper hyperfine coupling constant was observed. This suggested a perturbation on the catalytic site after immobilization due to pH variation of the enzymatic microenvironments, thus influencing performance of laccase immobilized on nanozeolites.-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionPhysics Department Institute of Biosciences Letters and Exact Sciences – IBILCE/São Paulo State University – UNESP, São José do Rio Preto-
Descrição: dc.descriptionCentre for Natural Products Discovery School of Pharmacy and Biomolecular Science Liverpool John Moores University James Parsons Building, Byrom Street-
Descrição: dc.descriptionPhysics Department Institute of Biosciences Letters and Exact Sciences – IBILCE/São Paulo State University – UNESP, São José do Rio Preto-
Descrição: dc.descriptionFAPESP: 2016/24303-0-
Descrição: dc.descriptionFAPESP: 2018/21483-3-
Descrição: dc.descriptionCNPq: 406761/2013-2-
Descrição: dc.descriptionCNPq: 465594/2014-0-
Descrição: dc.descriptionCNPq: RF-2019-474\4-
Idioma: dc.languageen-
Relação: dc.relationApplied Catalysis A: General-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectEPR-
Palavras-chave: dc.subjectGlycerol-
Palavras-chave: dc.subjectImmobilization-
Palavras-chave: dc.subjectLaccase-
Palavras-chave: dc.subjectNanozeolites-
Palavras-chave: dc.subjectOxidation-
Título: dc.titleNanozeolites as support for laccase immobilization: Application to mediated glycerol oxidation-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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