[Preparation and charaterization of aminopolysterol immobilized invertase].

Invertase from Saccharomyces cerevisiae was immobilized on aminopolysterol by adsorption, glutaraldehyde, carbodiimide or bromacetyl methods. The dependence of activity of invertase immobilized by the carbodiimide method upon pH, temperature and sucrose concentration was studied. The "effective" Michaelis constant of the immobilized preparation was 6 times higher than that of soluble inverase. At high sucrose concentrations (beginning with 0.2 M for immobilized and 0.9 M for soluble invertase) substrate inhibition was observed. The data on stability of immobilized invertase during refrigerated storage and in a working flow column were obtained.