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 | Acesso ao texto completo restrito à biblioteca da Embrapa Agroindústria Tropical. Para informações adicionais entre em contato com cnpat.biblioteca@embrapa.br. |
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Registro Completo |
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Biblioteca(s): |
Embrapa Agroindústria Tropical. |
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Data corrente: |
04/06/2025 |
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Data da última atualização: |
04/06/2025 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
CAMPOS, A. S.; JESUS, E. da C.; MENDES FILHO, P. F.; ARAÚJO PEREIRA, A. P. DE; CASTRO, A. C. R. de; COELHO, A. C. M. A.; BORDALLO, P. do N.; BORGES, W. L.; CARVALHO, A. C. P. P. de. |
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Afiliação: |
ARLENE SANTISTEBAN CAMPOS, UNIVERSITY OF SÃO PAULO; EDERSON DA CONCEICAO JESUS, CNPAB; PAULO FURTADO MENDES FILHO, FEDERAL UNIVERSITY OF CEARÁ; ARTHUR PRUDÊNCIO DE ARAÚJO PEREIRA, FEDERAL UNIVERSITY OF CEARÁ; ANA CECILIA RIBEIRO DE CASTRO, CNPAT; ARTHUR CESAR MINA ALBUQUERQUE COELHO, FEDERAL INSTITUTE OF EDUCATION SCIENCE AND TECHNOLOGY OF CEARÁ, PECÉM; PATRICIA DO NASCIMENTO BORDALLO, CNPAT; WARDSSON LUSTRINO BORGES, CNPAT; ANA CRISTINA PORTUGAL P DE CARVALHO, CNPAT. |
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Título: |
A New Multi-Active Heterogeneous Biocatalyst Prepared Through a Layer-by-Layer Co-Immobilization Strategy of Lipase and Laccase on Nanocellulose-Based Materials. |
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Ano de publicação: |
2025 |
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Fonte/Imprenta: |
Applied Soil Ecology, 211, 106102 , 2025. |
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DOI: |
https://doi.org/10.3390/ catal15020099 |
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Idioma: |
Inglês |
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Conteúdo: |
Lipase from Pseudomonas fl uorescens (PFL) and laccase from Trametes versicolor were co-immobilized onto nanocellulose (NC), using a layer-by-layer approach. Initially, PFL was adsorbed onto NC through ionic and hydrophobic interactions. To achieve higher PFL immobilization yield and activity, NC was functionalized with aldehyde groups through periodate oxidation (NCox) or glutaraldehyde activation (NC-GA). FTIR analysis confi rmed these chemical modifi cations. Among the functionalized NCs, NCox showed the best capacity to retain higher amounts of PFL (maximum load: 20 mg/g), and this support was selected to proceed with the co-immobilization experiments. In this process, NCox-250-PFL (NCox activated with 250 µmol/g of aldehyde groups) was covered with polyethyleneimine (PEI), laccase was co-immobilized, and a crosslinking step using glutaraldehyde was used to covalently attach the enzymes to the support, producing the biocatalyst NCox-250-PFL-PEI-Lac-GA. Co-immobilized enzymes presented higher thermal stability (50 ◦ C) than soluble enzymes; co-immobilized laccase retained 61.1% of its activity after 24 h, and PFL retained about 90% after 48 h of deactivation at 50 ◦ C. In operational stability assays, the heterogeneous biocatalysts maintained more than 45% of their activity after fi ve cycles of pNPB hydrolysis and ABTS oxidation. This co-immobilized biocatalyst, with its high stability and activity retention, is a promising multi-active heterogeneous biocatalyst for use in cascade reactions of industrial interest. MenosLipase from Pseudomonas fl uorescens (PFL) and laccase from Trametes versicolor were co-immobilized onto nanocellulose (NC), using a layer-by-layer approach. Initially, PFL was adsorbed onto NC through ionic and hydrophobic interactions. To achieve higher PFL immobilization yield and activity, NC was functionalized with aldehyde groups through periodate oxidation (NCox) or glutaraldehyde activation (NC-GA). FTIR analysis confi rmed these chemical modifi cations. Among the functionalized NCs, NCox showed the best capacity to retain higher amounts of PFL (maximum load: 20 mg/g), and this support was selected to proceed with the co-immobilization experiments. In this process, NCox-250-PFL (NCox activated with 250 µmol/g of aldehyde groups) was covered with polyethyleneimine (PEI), laccase was co-immobilized, and a crosslinking step using glutaraldehyde was used to covalently attach the enzymes to the support, producing the biocatalyst NCox-250-PFL-PEI-Lac-GA. Co-immobilized enzymes presented higher thermal stability (50 ◦ C) than soluble enzymes; co-immobilized laccase retained 61.1% of its activity after 24 h, and PFL retained about 90% after 48 h of deactivation at 50 ◦ C. In operational stability assays, the heterogeneous biocatalysts maintained more than 45% of their activity after fi ve cycles of pNPB hydrolysis and ABTS oxidation. This co-immobilized biocatalyst, with its high stability and activity retention, is a promising multi-active heterogeneous biocatalyst for use ... Mostrar Tudo |
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Palavras-Chave: |
Ativação de glutaraldeído; Co-immobilization; Co-imobilização; Glutaraldehyde activation; Lacase; Nanocellulose; Nanocelulose; Oxidação de periodato; Periodate oxidation. |
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Thesagro: |
Enzima; Lípase. |
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Thesaurus Nal: |
Enzymes; Laccase. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02753naa a2200385 a 4500
001 2176427
005 2025-06-04
008 2025 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.3390/ catal15020099$2DOI
100 1 $aCAMPOS, A. S.
245 $aA New Multi-Active Heterogeneous Biocatalyst Prepared Through a Layer-by-Layer Co-Immobilization Strategy of Lipase and Laccase on Nanocellulose-Based Materials.$h[electronic resource]
260 $c2025
520 $aLipase from Pseudomonas fl uorescens (PFL) and laccase from Trametes versicolor were co-immobilized onto nanocellulose (NC), using a layer-by-layer approach. Initially, PFL was adsorbed onto NC through ionic and hydrophobic interactions. To achieve higher PFL immobilization yield and activity, NC was functionalized with aldehyde groups through periodate oxidation (NCox) or glutaraldehyde activation (NC-GA). FTIR analysis confi rmed these chemical modifi cations. Among the functionalized NCs, NCox showed the best capacity to retain higher amounts of PFL (maximum load: 20 mg/g), and this support was selected to proceed with the co-immobilization experiments. In this process, NCox-250-PFL (NCox activated with 250 µmol/g of aldehyde groups) was covered with polyethyleneimine (PEI), laccase was co-immobilized, and a crosslinking step using glutaraldehyde was used to covalently attach the enzymes to the support, producing the biocatalyst NCox-250-PFL-PEI-Lac-GA. Co-immobilized enzymes presented higher thermal stability (50 ◦ C) than soluble enzymes; co-immobilized laccase retained 61.1% of its activity after 24 h, and PFL retained about 90% after 48 h of deactivation at 50 ◦ C. In operational stability assays, the heterogeneous biocatalysts maintained more than 45% of their activity after fi ve cycles of pNPB hydrolysis and ABTS oxidation. This co-immobilized biocatalyst, with its high stability and activity retention, is a promising multi-active heterogeneous biocatalyst for use in cascade reactions of industrial interest.
650 $aEnzymes
650 $aLaccase
650 $aEnzima
650 $aLípase
653 $aAtivação de glutaraldeído
653 $aCo-immobilization
653 $aCo-imobilização
653 $aGlutaraldehyde activation
653 $aLacase
653 $aNanocellulose
653 $aNanocelulose
653 $aOxidação de periodato
653 $aPeriodate oxidation
700 1 $aJESUS, E. da C.
700 1 $aMENDES FILHO, P. F.
700 1 $aARAÚJO PEREIRA, A. P. DE
700 1 $aCASTRO, A. C. R. de
700 1 $aCOELHO, A. C. M. A.
700 1 $aBORDALLO, P. do N.
700 1 $aBORGES, W. L.
700 1 $aCARVALHO, A. C. P. P. de
773 $tApplied Soil Ecology, 211, 106102 , 2025.
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