Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions

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dc.contributor.authorKornecki, Jakub F.
dc.contributor.authorCarballares, Diego
dc.contributor.authorSterlinga, Roberto Morellon
dc.contributor.authorSiar, El Hocine
dc.contributor.authorKashefi, Saeid
dc.contributor.authorChafiaa, Mazri
dc.contributor.authorPeña, Sara Arana
dc.contributor.authorRios, Nathalia Saraiva
dc.contributor.authorGonçalves, Luciana Rocha Barros
dc.contributor.authorLafuente, Roberto Fernandez
dc.date.accessioned2021-11-29T21:30:36Z
dc.date.issued2020-08
dc.description.embargo2030-12
dc.description.resumoA destabilizing effect at pH 7 of sodium phosphate on several lipases immobilized via interfacial activation is shown in this work. This paper investigates if this destabilizing effect is extended to other inactivation conditions, immobilization protocols or even other immobilized enzymes (ficin, trypsin, β-galactosidase, β-glucosidase, laccase, glucose oxidase and catalase). As lipases, those from Candida antarctica (A and B), Candida rugosa and Rhizomucor miehei have been used. Results confirm the very negative effect of 100 mM sodium phosphate at pH 7.0 for the stability of all studied lipases immobilized on octyl agarose, while using glutaraldehyde-support the effect is smaller (still very significant using CALA) and in some cases the effect disappeared (e.g., using CALB). The change of the pH to 5.0 or 9.0, or the addition of 1 M NaCl reduced the negative effect of the phosphate in some instances (e.g., at pH 5.0, this negative effect is only relevant for CALB). Regarding the other enzymes, only the monomeric β-galactosidase from Aspergillus oryzae is strongly destabilized by the phosphate buffer. This way, the immobilization protocol and the inactivation conditions strongly modulate the negative effect of sodium phosphate on the stability of immobilized lipases, and this effect is not extended to other enzymespt_BR
dc.identifier.citationKORNECKI, Jakub F.; CARBALLARES, Diego; MORELLON-STERLING, Roberto; SIAR, El Hocine; KASHEFI, Saeid; CHAFIAA, Mazri; ARANA-PEÑA, Sara; RIOS, Nathalia S.; GONÇALVES, Luciana R.B.; FERNANDEZ-LAFUENTE, Roberto. Influence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditions. Process Biochemistry, [S.L.], v. 95, p. 288-296, ago. 2020. Disponível em: https://www.sciencedirect.com/science/article/abs/pii/S1359511320301161?via%3Dihub#!. Acesso em: 29 nov. 2021.https://doi.org/10.1016/j.procbio.2020.02.025pt_BR
dc.identifier.doi10.1016/j.procbio.2020.02.025
dc.identifier.issn1359-5113
dc.identifier.urihttps://repositorio.ufrn.br/handle/123456789/45070
dc.languageenpt_BR
dc.publisherElsevierpt_BR
dc.subjectLipase interfacial activationpt_BR
dc.subjectEnzyme destabilizationpt_BR
dc.subjectImmobilized enzyme stabilitypt_BR
dc.subjectBuffers and enzyme stabilitypt_BR
dc.subjectTuning enzyme stability by immobilizationpt_BR
dc.titleInfluence of phosphate anions on the stability of immobilized enzymes. Effect of enzyme nature, immobilization protocol and inactivation conditionspt_BR
dc.typearticlept_BR

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