Effects of enzyme loading and immobilization conditions on the catalytic features of lipase from pseudomonas fluorescens immobilized on Octyl-Agarose beads

Página do item simplificado Estatísticas
dc.contributor.authorPeña, Sara Arana
dc.contributor.authorRios, Nathalia Saraiva
dc.contributor.authorNavarro, Diego Carballares
dc.contributor.authorSanchez, Carmen Mendez
dc.contributor.authorLokha, Yuliya
dc.contributor.authorGonçalves, Luciana Rocha Barros
dc.contributor.authorLafuente, Roberto Fernandez
dc.date.accessioned2021-11-29T20:39:26Z
dc.date.available2021-11-29T20:39:26Z
dc.date.issued2020-02-28
dc.description.resumoThe lipase from Pseudomonas fluorescens (PFL) has been immobilized on octyl-agarose beads under 16 different conditions (varying pH, ionic strength, buffer, adding some additives) at two different loadings, 1 and 60 mg of enzyme/g of support with the objective of check if this can alter the biocatalyst features. The activity of the biocatalysts versus p-nitrophenyl butyrate and triacetin and their thermal stability were studied. The different immobilization conditions produced biocatalysts with very different features. Considering the extreme cases, using 1 mg/g preparations, PFL stability changed more than fourfolds, while their activities versus pNPB or triacetin varied a 50–60%. Curiously, PFL specific activity versus triacetin was higher using highly enzyme loaded biocatalysts than using lowly loaded biocatalysts (even by a twofold factor). Moreover, stability of the highly loaded preparations was higher than that of the lowly loaded preparations, in many instances even when using 5°C higher temperatures (e.g., immobilized in the presence of calcium, the highly loaded biocatalysts maintained after 24 h at 75°c a 85% of the initial activity, while the lowly loaded preparation maintained only 27% at 70°C). Using the highly loaded preparations, activity of the different biocatalysts versus pNPB varied almost 1.7-folds and versus triacetin 1.9-folds. In this instance, the changes in stability caused by the immobilization conditions were much more significant, some preparations were almost fully inactivated under conditions where the most stable one maintained more than 80% of the initial activity. Results suggested that immobilization conditions greatly affected the properties of the immobilized PFL, partially by individual molecule different conformation (observed using lowly loaded preparations) but much more relevantly using highly loaded preparations, very likely by altering some enzyme-enzyme intermolecular interactions. There is not an optimal biocatalyst considering all parameters. That way, preparation of biocatalysts using this support may be a powerful tool to tune enzyme features, if carefully controlledpt_BR
dc.identifier.citationARANA-PEÑA, Sara; RIOS, Nathalia S.; CARBALLARES, Diego; MENDEZ-SANCHEZ, Carmen; LOKHA, Yuliya; GONÇALVES, Luciana R. B.; FERNANDEZ-LAFUENTE, Roberto. Effects of Enzyme Loading and Immobilization Conditions on the Catalytic Features of Lipase From Pseudomonas fluorescens Immobilized on Octyl-Agarose Beads. Frontiers In Bioengineering And Biotechnology, [S.L.], v. 8, p. 1-2, 28 fev. 2020. Disponível em: https://www.frontiersin.org/articles/10.3389/fbioe.2020.00036/full. Acesso em: 29 nov. 2021. https://doi.org/10.3389/fbioe.2020.00036pt_BR
dc.identifier.doi10.3389/fbioe.2020.00036
dc.identifier.urihttps://repositorio.ufrn.br/handle/123456789/45065
dc.languageenpt_BR
dc.publisherFrontierspt_BR
dc.rightsAttribution 3.0 Brazil*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/br/*
dc.subjectImmobilization conditionspt_BR
dc.subjectProtein intermolecular interactionpt_BR
dc.subjectLipase modulationpt_BR
dc.subjectInterfacial activationpt_BR
dc.subjectLipase immobilizationpt_BR
dc.titleEffects of enzyme loading and immobilization conditions on the catalytic features of lipase from pseudomonas fluorescens immobilized on Octyl-Agarose beadspt_BR
dc.typearticlept_BR

Arquivos

Pacote Original

Agora exibindo 1 - 1 de 1
Nenhuma Miniatura disponível
Nome:
EffectsEnzymeLoading_Rios_2021.pdf
Tamanho:
1.46 MB
Formato:
Adobe Portable Document Format
Nenhuma Miniatura disponível
Baixar

Licença do Pacote

Agora exibindo 1 - 1 de 1
Nenhuma Miniatura disponível
Nome:
license.txt
Tamanho:
1.53 KB
Formato:
Item-specific license agreed upon to submission
Nenhuma Miniatura disponível
Baixar

Coleções

CT - DEQ - Artigos publicados em periódicos
Repositório Institucional - UFRN Campus Universitário Lagoa NovaCEP 59078-970 Caixa postal 1524 Natal/RN - BrasilUniversidade Federal do Rio Grande do Norte© Copyright 2025. Todos os direitos reservados.
Contato+55 (84) 3342-2260 - R232Setor de Repositórios Digitaisrepositorio@bczm.ufrn.br
DSpaceIBICT
OasisBR
LAReferencia
Customizado pela CAT - BCZM