Enhancement of Peroxidase Stability Against Oxidative Self-Inactivation by Co-immobilization with a Redox-Active Protein in Mesoporous Silicon and Silica Microparticles

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dc.contributor.authorSahare, P.
dc.contributor.authorOsorio Román, Igor
dc.contributor.authorAyala, M.
dc.contributor.authorVazquez-Duhalt, R.
dc.contributor.authorPal, U.
dc.contributor.authorLoni, A.
dc.contributor.authorCanham, L. T.
dc.contributor.authorAgarwal, V.
dc.date.accessioned2019-10-17T13:41:11Z
dc.date.available2019-10-17T13:41:11Z
dc.date.issued2016
dc.date.updated2019-10-14T19:22:23Z
dc.description.abstractAbstract The study of the stability enhancement of a peroxidase immobilized onto mesoporous silicon/silica microparticles is presented. Peroxidases tend to get inactivated in the presence of hydrogen peroxide, their essential co-substrate, following an auto-inactivation mechanism. In order to minimize this inactivation, a second protein was co-immobilized to act as an electron acceptor and thus increase the stability against self-oxidation of peroxidase. Two heme proteins were immobilized into the microparticles: a fungal commercial peroxidase and cytochrome c from equine heart. Two types of biocatalysts were prepared: one with only covalently immobilized peroxidase (one-protein system) and another based on covalent co-immobilization of peroxidase and cytochrome c (two-protein system), both immobilized by using carbodiimide chemistry. The amount of immobilized protein was estimated spectrophotometrically, and the characterization of the biocatalyst support matrix was performed using Brunauer–Emmett–Teller (BET), scanning electron microscopy with energy-dispersive X-ray spectroscopy (SEM-EDX), and Fourier transform infrared (FTIR) analyses. Stability studies show that co-immobilization with the two-protein system enhances the oxidative stability of peroxidase almost four times with respect to the one-protein system. Thermal stability analysis shows that the immobilization of peroxidase in derivatized porous silicon microparticles does not protect the protein from thermal denaturation, whereas biogenic silica microparticles confer significant thermal stabilization.Abstract The study of the stability enhancement of a peroxidase immobilized onto mesoporous silicon/silica microparticles is presented. Peroxidases tend to get inactivated in the presence of hydrogen peroxide, their essential co-substrate, following an auto-inactivation mechanism. In order to minimize this inactivation, a second protein was co-immobilized to act as an electron acceptor and thus increase the stability against self-oxidation of peroxidase. Two heme proteins were immobilized into the microparticles: a fungal commercial peroxidase and cytochrome c from equine heart. Two types of biocatalysts were prepared: one with only covalently immobilized peroxidase (one-protein system) and another based on covalent co-immobilization of peroxidase and cytochrome c (two-protein system), both immobilized by using carbodiimide chemistry. The amount of immobilized protein was estimated spectrophotometrically, and the characterization of the biocatalyst support matrix was performed using Brunauer–Emmett–Teller (BET), scanning electron microscopy with energy-dispersive X-ray spectroscopy (SEM-EDX), and Fourier transform infrared (FTIR) analyses. Stability studies show that co-immobilization with the two-protein system enhances the oxidative stability of peroxidase almost four times with respect to the one-protein system. Thermal stability analysis shows that the immobilization of peroxidase in derivatized porous silicon microparticles does not protect the protein from thermal denaturation, whereas biogenic silica microparticles confer significant thermal stabilization.
dc.fuente.origenBiomed Central
dc.identifier.citationNanoscale Research Letters. 2016 Sep 20;11(1):417
dc.identifier.doi10.1186/s11671-016-1605-4
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/26644
dc.issue.numeroNo. 417
dc.language.isoen
dc.pagina.final10
dc.pagina.inicio1
dc.revistaNanoscale Research Letterses_ES
dc.rightsacceso abierto
dc.rights.holderThe Author(s).
dc.subject.ddc570
dc.subject.deweyBiologíaes_ES
dc.subject.otherBiología celulares_ES
dc.subject.otherProteínas - Análisises_ES
dc.subject.otherPeroxidasases_ES
dc.titleEnhancement of Peroxidase Stability Against Oxidative Self-Inactivation by Co-immobilization with a Redox-Active Protein in Mesoporous Silicon and Silica Microparticleses_ES
dc.typeartículo
dc.volumenVol. 11
sipa.codpersvinculados207713
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