Immobilization of invertase in conducting thiophene-capped poly(methylmethacrylate)/polypyrrole matrices.
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.
Alkan
S
S
Department of Chemistry, Middle East Technical Univervity, Ankara, Turkey.
Toppare
L
L
Yagci
Y
Y
Hepuzer
Y
Y
D004553:Electric Conductivity; D004572:Electrolysis; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008855:Microscopy, Electron, Scanning; D011108:Polymers / Q000378:metabolism*; D019904:Polymethyl Methacrylate / Q000378:metabolism*; D011758:Pyrroles / Q000378:metabolism*; D013499:Surface Properties; D013696:Temperature; D013876:Thiophenes / Q000378:metabolism*; D043324:beta-Fructofuranosidase
D004800:Enzymes, Immobilized; D011108:Polymers; D011758:Pyrroles; D013876:Thiophenes; C067635:polypyrrole; D019904:Polymethyl Methacrylate; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase