[Kinetic properties of enzymes in particular of yeast alcohol dehydrogenase following their adsorption on polyaminomethylstyrene].
The adsorption of 8 enzymes to polyaminomethylstyrene was studied. While lactate dehydrogenase, alkaline phosphatase and glucose-6-phosphate dehydrogenase exhibit a relatively low affinity to the carrier, alcohol dehydrogenase, glutamate dehydrogenase and urease were found to form stabile complexes with the polymer that are enzymatically active. Adsorbed urease and beta-hydroxybutyrate dehydrogenase, are still active after several weeks; the other preparations lose their activity soon. It can be shown by the example of yeast alcohol dehydrogenase that the activity loss following adsorption is caused possibly by a process of reorientation of already bound enzyme molecules or by the increasing enzyme coverage of the carrier, with the active centres becoming more and more inaccessible for the substrate. During the substrate conversion catalysed by the alcohol dehydrogenase-polyaminomethylstyrene complex, a small amount of the enzyme is again detached from the carrier. The activity rises to a certain extent in the supernatant but drops to zero again. The stability of the adsorbed urease is distinctly increased compared with the dissolved enzyme. For the pH optimum and the KM value there are no differences between the two preparations. Continuous application of polyaminomethylstyrene-bound beta-hydroxybutyrate dehydrogenase and urease, respectively, in a column shows that both preparations have unchanged enzymatic activities even after running times of 5 and 24 days, respectively.
D000327:Adsorption; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D001665:Binding Sites; D002021:Buffers; D002384:Catalysis; D007700:Kinetics; D013343:Styrenes; D015003:Yeasts / Q000201:enzymology*
D002021:Buffers; D013343:Styrenes; D000429:Alcohol Oxidoreductases
Kinetische Eigenschaften von Enzymen, insbesondere der Hefe-Alkohol-dehydrogenase, nach ihrer Adsorption an Polyaminomethylstyrol