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. © 2010 The Royal Society of Chemistry.
Enzyme-functionalized polymer brush films on the inner wall of silicon-glass microreactors with tunable biocatalytic activity / Costantini, F.; Benetti, E. M.; Reinhoudt, D. N.; Huskens, J.; Vancso, G. J.; Verboom, W.. - In: LAB ON A CHIP. - ISSN 1473-0197. - 10:24(2010), pp. 3407-3412. [10.1039/c0lc00187b]
Enzyme-functionalized polymer brush films on the inner wall of silicon-glass microreactors with tunable biocatalytic activity
Costantini F.Primo
;
2010
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. © 2010 The Royal Society of Chemistry.File | Dimensione | Formato | |
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