Issue 38, 2015

Silk fibroin hydroxyapatite composite thermal stabilisation of carbonic anhydrase

Abstract

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.

Graphical abstract: Silk fibroin hydroxyapatite composite thermal stabilisation of carbonic anhydrase

Article information

Article type
Communication
Submitted
16 Jul 2015
Accepted
24 Aug 2015
First published
24 Aug 2015

J. Mater. Chem. A, 2015,3, 19282-19287

Author version available

Silk fibroin hydroxyapatite composite thermal stabilisation of carbonic anhydrase

J. H. Lopes, M. Guilhou, B. Marelli, F. G. Omenetto, D. L. Kaplan, J. E. Barralet and G. Merle, J. Mater. Chem. A, 2015, 3, 19282 DOI: 10.1039/C5TA05397H

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