ABSTRACT
An optimal, in respect to productivity (activity X stability), enzyme ratio for immobilization of multienzyme systems was calculated by using the kinetic parameters (KM and Vmax), data on the stability and yield of each enzyme during immobilization. The experimental data, obtained during combined immobilization of invertase, mutarotase and glucose oxidase, illustrate the theoretical propositions.
Subject(s)
Enzymes, Immobilized/metabolism , Animals , Carbohydrate Epimerases/metabolism , Dose-Response Relationship, Drug , Glucose Oxidase/metabolism , Glycoside Hydrolases/metabolism , Kidney/enzymology , Kinetics , Mathematics , Penicillium/enzymology , Saccharomyces cerevisiae/enzymology , Substrate Specificity , Swine , beta-FructofuranosidaseABSTRACT
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.
Subject(s)
Enzymes, Immobilized/metabolism , Saccharomyces cerevisiae/enzymology , Sucrase/metabolism , Kinetics , PolymersABSTRACT
Immobilization and thermostability of glucose oxidase immobilized on silica gel MCA-750 7 by different methods were studied. The process of inactivation was found to follow two stages that differed in their rate. The most stable preparations were produced by immobilization based on bromacetyl and glutaraldehyde methods.
