Issue 24, 2010

Enzyme-functionalized polymer brush films on the inner wall of silicon–glass microreactors with tunable biocatalytic activity

Abstract

The lipase from Candida Rugosa was immobilized to a poly(methacrylic acid) polymer brush layer, grown on the inner wall of silicon–glass microreactors. The hydrolysis of 4-nitrophenyl acetate was used as a model reaction to study the activity of this biocatalytic system. The amount of bound lipase could be tuned by changing the polymerization time of the brush formation. The Michaelis–Menten constants and Vmax values, determined for immobilized and free lipase, are similar, demonstrating that the lipase's substrate affinity and its activity remain unchanged upon immobilization to the microchannel wall.

Graphical abstract: Enzyme-functionalized polymer brush films on the inner wall of silicon–glass microreactors with tunable biocatalytic activity

Supplementary files

Additions and corrections

Article information

Article type
Paper
Submitted
09 Jul 2010
Accepted
09 Sep 2010
First published
13 Oct 2010

Lab Chip, 2010,10, 3407-3412

Enzyme-functionalized polymer brush films on the inner wall of silicon–glass microreactors with tunable biocatalytic activity

F. Costantini, E. M. Benetti, D. N. Reinhoudt, J. Huskens, G. J. Vancso and W. Verboom, Lab Chip, 2010, 10, 3407 DOI: 10.1039/C0LC00187B

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