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

Lab Chip. 2010 Dec 21;10(24):3407-12. doi: 10.1039/c0lc00187b. Epub 2010 Oct 13.

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 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biocatalysis*
  • Bioreactors*
  • Candida / metabolism*
  • Catalysis
  • Enzymes, Immobilized
  • Fungal Proteins / chemistry*
  • Kinetics
  • Lipase / chemistry
  • Microscopy, Atomic Force / methods
  • Models, Chemical
  • Polymers / chemistry*
  • Silicon / chemistry*
  • Time Factors

Substances

  • Enzymes, Immobilized
  • Fungal Proteins
  • Polymers
  • Lipase
  • Silicon