Enhancement of the catalytic activity of Carbonic Anhydrase by covalent immobilization on Magnetic Cellulose Crystals

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dc.contributor.authorRodriguez Liliana Castro
dc.contributor.authorRestrepo-Sanchez Nora
dc.contributor.authorPelaez Carlos
dc.contributor.authorBernal Claudia
dc.date.accessioned2025-05-19T21:46:10Z
dc.date.available2025-05-19T21:46:10Z
dc.date.issued2023/02/01
dc.description.abstractIn this study, Magnetic Cellulose Crystals (MCCs) are modified, characterized and used to immobilization of Bovine Carbonic Anhydrase (BCA). BCA enzyme was covalently attached via glutaraldehyde to two MCCs materials: a magnetic cellulose I polymorph (MCC-I) and a mixture of magnetic cellulose I and II polymorphs (MCCI-II). The esterase activity of BCA immobilized into MCC-I (BCA-MCC-I) and MCC-I-II (BCA-MCC-I-II) was 228 and 318 % greater than the free enzyme, respectively. At 60 degrees C, BCA-MCC-I-II maintained up to 80 % of its initial activity, after 48 h. The activity of BCA-MCC-I was higher in comparison with the other derivatives at acid pH, conserved the 80 % of initial activity after 48 h. The high activity and stability of achieved biocatalysts are considering a great starting step to develop green strategies for CO2 mitigation, using eco-friendly materials, like cellulose. These findings are expected to impact enzyme-based CO2 transformation strategies and contribute to mitigate global warming.
dc.identifier.doi10.1016/j.biteb.2023.101380
dc.identifier.urihttps://publicacionesabiertas.userena.cl/handle/123456789/347
dc.languageEnglish
dc.subjectTHERMAL-PROPERTIES, SODIUM-HYDROXIDE, CHITOSAN, NANOCRYSTALS, INHIBITION, CHITIN, PH, POLYMORPHS, SILICA, ENZYME
dc.titleEnhancement of the catalytic activity of Carbonic Anhydrase by covalent immobilization on Magnetic Cellulose Crystals
dc.typeArticle

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