Logo do repositório
 
Publicação

Biocatalytic CO2 absorption and structural studies of carbonic anhydrase under industrially-relevant conditions

2020-04-22Artigo científico Acesso aberto
Ver registo simples
dc.contributor.authorDe Castro, Aline M.
dc.contributor.authorFerreira, Elisabete
dc.contributor.authorPortugal, Carla
dc.contributor.authorNeves, Luisa A.
dc.contributor.authorCrespo, João G.
dc.contributor.institutionLAQV@REQUIMTE
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.pblMDPI - Multidisciplinary Digital Publishing Institute
dc.date.accessioned2021-06-25T22:17:56Z
dc.date.available2021-06-25T22:17:56Z
dc.date.issued2020-04-22
dc.descriptionUIDB/50006/2020 IF/00505/2014/CP1224/CT0004
dc.description.abstractThe unprecedently high CO2 levels in the atmosphere evoke the urgent need for development of technologies for mitigation of its emissions. Among the alternatives, the biocatalytic route has been claimed as one of the most promising. In the present work, the carbonic anhydrase from bovine erythrocytes (BCA) was employed as a model enzyme for structural studies in an aqueous phase at alkaline pH, which is typical of large-scale absorption processes under operation. Circular dichroism (CD) analysis revealed a high enzymatic stability at pH 10 with a prominent decrease of the melting temperature above this value. The CO2 absorption capacity of the aqueous solutions were assessed by online monitoring of pressure decay in a stainless-steel cell, which indicated a better performance at pH 10 with a kinetic rate increase of up to 43%, as compared to non-biocatalytic conditions. Even low enzyme concentrations (0.2 mg g−1) proved to be sufficient to improve the overall CO2 capture process performance. The enzyme-enhanced approach of CO2 capture presents a high potential and should be further studied.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent2103195
dc.identifier.doi10.3390/ijms21082918
dc.identifier.issn1661-6596
dc.identifier.otherPURE: 28981029
dc.identifier.otherPURE UUID: 95a71d64-cf2c-470c-b6e3-051f6d1bede0
dc.identifier.otherScopus: 85084031308
dc.identifier.otherPubMed: 32331206
dc.identifier.otherORCID: /0000-0002-9620-6286/work/91554808
dc.identifier.otherORCID: /0000-0001-8714-3781/work/91554883
dc.identifier.otherPubMedCentral: PMC7215295
dc.identifier.otherWOS: 000535565300260
dc.identifier.urihttp://hdl.handle.net/10362/120023
dc.identifier.urlhttps://www.scopus.com/pages/publications/85084031308
dc.language.isoeng
dc.peerreviewedyes
dc.subjectCarbonic anhydrase
dc.subjectCircular dichroism
dc.subjectCO capture
dc.subjectFluorescence
dc.subjectGreenhouse gases
dc.subjectCatalysis
dc.subjectMolecular Biology
dc.subjectSpectroscopy
dc.subjectComputer Science Applications
dc.subjectPhysical and Theoretical Chemistry
dc.subjectOrganic Chemistry
dc.subjectInorganic Chemistry
dc.titleBiocatalytic CO2 absorption and structural studies of carbonic anhydrase under industrially-relevant conditionsen
dc.typejournal article
degois.publication.issue8
degois.publication.titleInternational Journal of Molecular Sciences
degois.publication.volume21
dspace.entity.typePublication
rcaap.rightsopenAccess

Ficheiros

Principais
A mostrar 1 - 1 de 1
Miniatura
Nome:
ijms_21_02918.pdf
Tamanho:
2.01 MB
Formato:
Adobe Portable Document Format
Ver/Abrir

Coleções

FCT: DQ - Artigos em revista internacional com arbitragem científica