Abstract
Amyloglucosidase (AMG) was immobilized on four different inorganic supports, two controlled-pore glasses (CPG, 170 and 729 Å), one ceramic silica support (Micropil A) and one alumina-based surface porous support (Biotage), by silanization followed by glutaraldehyde activation. The alumina-based support, Biotage, was also used for immobilization with polyethylenimine functionalization followed by glutaraldehyde activation. A thermostable α-amylase, Termamyl, was immobilized on three different supports, CPG of 1489 Å, Biotage and Micropil A, by silanization and glutaraldehyde activation. The different immobilized supports were packed into identical reactors (30 μl). The AMG supports were investigated regarding immobilization efficiency and the optimum pore size necessary for the entry of a high-molecular-weight substrate (glycogen) so that optimum activity could be obtained. The highest immobilization efficiency was obtained on CPG of 170 Å, but the highest activity was obtained on CPG of 729 Å. The three Termamyl supports were compared and the highest immobilization efficiency was obtained on Micropil A, but the highest enzyme activity was obtained on CPG of 1489 Å followed by Biotage.
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