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

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...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2012-01, Vol.48 (9), p.1314-1316
Main Authors: Emond, Stéphane, Guieysse, David, Lechevallier, Severine, Dexpert-Ghys, Jeannette, Monsan, Pierre, Remaud-Siméon, Magali
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biomimetic Materials - chemistry
Biomimetics
Chemical Precipitation
Diatoms - chemistry
Diatoms - enzymology
Enzyme Activation
Enzyme Stability
Enzymes, Immobilized - chemistry
Enzymes, Immobilized - metabolism
Esterases - chemistry
Esterases - metabolism
Life Sciences
Lipase - chemistry
Lipase - metabolism
Molecular Sequence Data
Peptides - chemistry
Silicon Dioxide - chemistry
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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.
ISSN:1359-7345
1364-548X
DOI:10.1039/c1cc14478b