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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Silk fibroin hydroxyapatite composite thermal stabilisation of carbonic anhydrase

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Author(s):
Lopes, J. H. [1] ; Guilhou, M. [1] ; Marelli, B. [2] ; Omenetto, F. G. [2] ; Kaplan, D. L. [2] ; Barralet, J. E. [1, 3] ; Merle, G. [1]
Total Authors: 7
Affiliation:
[1] McGill Univ, Fac Dent, Montreal, PQ H3A 2B2 - Canada
[2] Tufts Univ, Dept Biomed Engn, Medford, MA 02155 - USA
[3] McGill Univ, Fac Med, Dept Surg, Montreal, PQ H3A 2B2 - Canada
Total Affiliations: 3
Document type: Journal article
Source: JOURNAL OF MATERIALS CHEMISTRY A; v. 3, n. 38, p. 19282-19287, 2015.
Web of Science Citations: 7
Abstract

Carbonic anhydrase was entrapped in a matrix of ultrasonically bonded hydroxyapatite microparticles coated with beta-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 degrees C and the assembly retained 45% of its initial activity after 3 weeks of continuous heating at 80 degrees 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. (AU)

FAPESP's process: 13/12376-5 - Bone formation controlled by biologically active inorganic ions: investigation of the role and controlled delivery of relevant ions from biomaterials
Grantee:João Henrique Lopes
Support Opportunities: Scholarships abroad - Research Internship - Doctorate