Immobilization of invertase in conducting thiophene-capped poly(methylmethacrylate)/polypyrrole matrices

J Biomater Sci Polym Ed. 1999;10(12):1223-35. doi: 10.1163/156856299x00036.

Abstract

Immobilization of invertase in thiophene-capped poly(methylmethacrylate)/polypyrrole matrices was achieved by constant potential electrolysis using different supporting electrolytes. Optimum reaction conditions such as substrate concentration, temperature, and pH for the enzyme electrodes were determined. The temperature and pH were found to be 60 degrees C and 4.8, respectively. The effect of supporting electrolyte on the enzyme activity revealed that SDS was the best in the immobilization procedure. Michaelis-Menten constant and the maximum reaction rate in PMMA/PPy matrices were of the order of that of pristine polypyrrole. However, in terms of repeated use, the copolymer matrices were superior to polypyrrole.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Electric Conductivity
  • Electrolysis
  • Enzymes, Immobilized / metabolism*
  • Glycoside Hydrolases / metabolism*
  • Hydrogen-Ion Concentration
  • Kinetics
  • Microscopy, Electron, Scanning
  • Polymers / metabolism*
  • Polymethyl Methacrylate / metabolism*
  • Pyrroles / metabolism*
  • Surface Properties
  • Temperature
  • Thiophenes / metabolism*
  • beta-Fructofuranosidase

Substances

  • Enzymes, Immobilized
  • Polymers
  • Pyrroles
  • Thiophenes
  • polypyrrole
  • Polymethyl Methacrylate
  • Glycoside Hydrolases
  • beta-Fructofuranosidase