Immobilization of invertase by encapsulation in polyelectrolyte complexes.
Free and polystyrene-bound invertase from Saccharomyces cerevisiae were encapsulated within symplex membranes which were composed of cellulose sulfate as the polymeric anion and poly(dimethyldiallylammonium chloride) as the polymeric cation. The kinetics and the performance of the encapsulated enzyme preparations have been compared to the free enzyme employing the hydrolysis of sucrose. The pH and temperature optima were only slightly affected by the encapsulation. The kinetic constants, however, were changed by the encapsulation as a result of diffusional limitation. Encapsulated invertase showed a high storage stability and a high operational stability if low substrate concentrations were applied. The coimmobilization of invertase with living cells, which are not capable of utilizing sucrose, in the described capsules, opens many possibilities in fermentation technology.
Martin-Luther University, Department of Biotechnology, Halle, GDR.
J
J
Mansfeld
M
M
Förster
A
A
Schellenberger
H
H
Dautzenberg
D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000378:metabolism*; D007700:Kinetics; D008567:Membranes, Artificial; D011137:Polystyrenes; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013816:Thermodynamics; D043324:beta-Fructofuranosidase
D004800:Enzymes, Immobilized; D008567:Membranes, Artificial; D011137:Polystyrenes; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase