PG-EAM - Programa de Pós-Graduação em Engenharia Aeronáutica e Mecânica
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Artigo 2015

Silk fibroin hydroxyapatite composite thermal stabilisation of carbonic anhydrase

Autores

Guilhou, M.
Marelli, B.
Omenetto, F. G.
Kaplan, D. L.
Barralet, J. E.
Merle, G.

Journal of Materials Chemistry A , vol. 3 , no. 38 , pp. 19282-19287

ISSN: 20507488

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Citações
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Autores

Resumo

© The Royal Society of Chemistry 2015.Carbonic anhydrase was entrapped in a matrix of ultrasonically bonded hydroxyapatite microparticles coated with β-sheet structured silk fibroin. Transfer of the reactant and product between the enzyme and the assembly surface was evident and the system showed a remarkable operational, storage and thermal stability, with enzymatic activity almost unchanged after a one hour's treatment at 110 °C and the assembly retained 45% of its initial activity after 3 weeks of continuous heating at 80 °C in an amine solution. This thermal stability was excellent compared with described CA immobilization systems and indicates that silk fibroin may limit thermally induced enzyme conformation changes and prevent desorption.

Chemistry (all) (CHEM) Renewable Energy, Sustainability and the Environment (ENER) Materials Science (all) (MATE)
: Scopus
Última atualização: 2026-06-25
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