Abstract
Mushroom tyrosinase immobilization on controlled pore glass with three different functional groups like alkylamino, carboxyl and arylamino is performed. The effect of the alkylamino-CPG arm extension on enzymatic stability and catalytic activity is also investigated. The results expressed in terms of ligand coupling, % yield and kinetic parameters, like the apparent Km app and Vmax app and the inherent Km inh and Vmax inh values demonstrate the best performance of tyrosinase immobilized on alkylammino-CPGs.
Original language | English |
---|---|
Pages (from-to) | 48-54 |
Number of pages | 7 |
Journal | Sensors and Actuators, B: Chemical |
Volume | 125 |
Issue number | 1 |
DOIs | |
Publication status | Published - Jul 16 2007 |
Keywords
- Bioreactor
- Controlled pore glass
- Kinetic parameters
- Tyrosinase immobilization
ASJC Scopus subject areas
- Analytical Chemistry
- Electrochemistry
- Electrical and Electronic Engineering