Issue 9, 2012

Alteration of enzyme activity and enantioselectivity by biomimetic encapsulation in silica particles

Abstract

Direct encapsulation of esterase or lipase fused with the silica-precipitating R5 peptide from Cylindrotheca fusiformis in silica particles afforded high yields of active entrapped protein. The hydrolytic activity of both enzymes against p-nitrophenyl butyrate was similarly affected by encapsulation and the enantioselectivity of the esterase was both improved and inverted.

Graphical abstract: Alteration of enzyme activity and enantioselectivity by biomimetic encapsulation in silica particles

Supplementary files

Article information

Article type
Communication
Submitted
22 Jul 2011
Accepted
26 Oct 2011
First published
12 Dec 2011

Chem. Commun., 2012,48, 1314-1316

Alteration of enzyme activity and enantioselectivity by biomimetic encapsulation in silica particles

S. Emond, D. Guieysse, S. Lechevallier, J. Dexpert-Ghys, P. Monsan and M. Remaud-Siméon, Chem. Commun., 2012, 48, 1314 DOI: 10.1039/C1CC14478B

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