Journal
LAB ON A CHIP
Volume 10, Issue 24, Pages 3407-3412Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c0lc00187b
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Funding
- Dutch Ministry of Economic Affairs
- Biopolysurf Marie Curie research network of the EU
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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 V-max 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.
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