Collect. Czech. Chem. Commun. 1986, 51, 2924-2932

Endopolygalacturonase immobilized on ceramic materials substituted with aminopropyl groups. Synthesis, kinetics, and mode of action

Lubomíra Rexová-Benkováa, Eva Stratilováa and Martin Čapkab

a Institute of Chemistry, Slovak Academy of Sciences, 842 38 Bratislava
b Institute of Chemical Process Fundamentals, Czechoslovak Academy of Sciences, 165 02 Prague 6-Suchdol


Endopolygalacturonase was immobilized on ground porous tiles and on ceramic rings functionalized with 3-(aminopropyl)triethoxysilane and glutaraldehyde. The relative activity of the immobilized enzymes depended on loading, attaining 32.4% for porous tiles and 44.0% for ceramic rings. The immobilization resulted in the shift of the optimum of enzyme performance to lower pH values, the temperature optimum increasing from 40 to 60 °C, along with thermostability. Immobilized enzymes showed constant activity during 8-months (porous tiles) and 3-months continuous percolation with 0.5% sodium pectate solution. In both cases, the immobilization resulted in preferential cleavage of glycosidic bonds at the end of the chain of high molecular substrate and in nonspecific cleavage of tetra(D-galactosiduronic acid).