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dc.contributor.author Ores, Joana da Costa
dc.contributor.author Sala, Luisa
dc.contributor.author Cerveira, Guido Picaluga
dc.contributor.author Kalil, Susana Juliano
dc.date.accessioned 2014-09-30T00:08:08Z
dc.date.available 2014-09-30T00:08:08Z
dc.date.issued 2012
dc.identifier.citation ORES, Joana da Costa et al. Purification of carbonic anhydrase from bovine erythrocytes and its application in the enzymic capture of carbon dioxide. Chemosphere, v. 88, p. 255–259, 2012. Disponível em: <http://www.sciencedirect.com/science/article/pii/S0045653512004110>. Acesso em: 09 set. 2014. pt_BR
dc.identifier.issn 0045-6535
dc.identifier.uri http://repositorio.furg.br/handle/1/4623
dc.description.abstract This work presents a study of industrially applicable techniques to obtain a biologically supported carbon dioxide capture system, based on the extraction of carbonic anhydrase from bovine blood. Carbonic anhydrase is a metalloenzyme which catalyzes the reversible hydration of carbon dioxide. The objective of this study was to establish conditions to obtain carbonic anhydrase from bovine erythrocytes and apply it in the capture of carbon dioxide. To achieve this, two different purification techniques were evaluated: one by extraction with the organic solvents chloroform and ethanol, where different solvent proportions were studied; and the other by ammonium sulfate precipitation, testing percent saturations between 10% and 80%. Carbon dioxide was enzymatically captured by its precipitation as calcium carbonate with the enzyme obtained by both techniques. The enzyme extracted by ethanol and chloroform showed an activity of 2623 U mL 1, recovery of 98% and purification factor of 104-fold. That precipitated by ammonium sulfate showed an activity of 2162 U mL 1, recovery of 66% and purification factor of 1.4-fold using 60% ammonium sulfate saturation. The results obtained in the carbon dioxide capture experiments showed that the carbonic anhydrase extracted in this study not only enhanced the hydration of CO2, but also promoted the formation of CaCO3. pt_BR
dc.language.iso eng pt_BR
dc.rights open access pt_BR
dc.subject Carbonic anhydrase pt_BR
dc.subject CO2 capture pt_BR
dc.subject Enzymically catalyzed capture pt_BR
dc.subject Precipitation pt_BR
dc.subject Organic solvents pt_BR
dc.subject Ammonium sulfate pt_BR
dc.title Purification of carbonic anhydrase from bovine erythrocytes and its application in the enzymic capture of carbon dioxide pt_BR
dc.type article pt_BR
dc.identifier.doi http://dx.doi.org/10.1016/j.chemosphere.2012.03.059 pt_BR


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