Related Experiment Videos
Immobilization of isochorismate hydroxymutase. Comparison of native versus immobilized enzyme
P M Schaaf1, L E Heide, E W Leistner
1Institut für Pharmazeutische Biologie, Rheinischen Friederich-Wilhelms-Universität Bonn, Germany.
Abstract:
Partially purified isochorismate hydroxymutase (isochorismate synthase, E.C. 5.4.99.6) from Flavobacterium K3-15, a vitamin K overproducer, was immobilized on CNBr-activated Sepharose 4B, alkylamine glass substituted with glutardialdehyde, and aminohexyl Sepharose 4B substituted with glutardialdehyde. The immobilized enzyme exhibited a lower specific activity but a broader pH tolerance and a higher thermostability than the soluble enzyme. The stability of the enzyme was greatly increased by immobilization. Isochorismic acid, which is not commercially available, was prepared by a constant flow incubation.