Endopolygalacturonase immobilized on ceramic materials substituted with aminopropyl groups. Synthesis, kinetics, and mode of action
- 1 January 1986
- journal article
- Published by Institute of Organic Chemistry & Biochemistry in Collection of Czechoslovak Chemical Communications
- Vol. 51 (12) , 2924-2932
- https://doi.org/10.1135/cccc19862924
Abstract
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).Keywords
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