Alteration of enzyme activity and enantioselectivity by biomimetic encapsulation in silica particlesElectronic supplementary information (ESI) available. See DOI: 10.1039/c1cc14478b

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 encapsulatio...

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Main Authors: Emond, Stphane, Guieysse, David, Lechevallier, Severine, Dexpert-Ghys, Jeannette, Monsan, Pierre, Remaud-Simon, Magali
Format: Article
Language:English
Online Access:Get full text
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Summary: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. Direct encapsulation into silica particles of Pseudomonas fluorescens esterase fused with the R5 peptide derived from Cylindrotheca fusiformis silaffin affected both hydrolytic activity and enantiopreference compared to the free enzyme.
ISSN:1359-7345
1364-548X
DOI:10.1039/c1cc14478b