Immobilization of isochorismate hydroxymutase. Comparison of native versus immobilized enzyme.
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.
Schaaf
P M
PM
Institut für Pharmazeutische Biologie, Rheinischen Friederich-Wilhelms-Universität Bonn, Germany.
Heide
L E
LE
Leistner
E W
EW
Tani
Y
Y
el-Olemy
M M
MM
D002384:Catalysis; D002827:Chorismic Acid / Q000737:chemistry; D003067:Coenzymes / Q000737:chemistry; D053138:Cyclohexenes; D004800:Enzymes, Immobilized / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D019751:Intramolecular Transferases; D007535:Isomerases / Q000737:chemistry*; D007700:Kinetics; D008274:Magnesium / Q000737:chemistry; D011506:Proteins / Q000378:metabolism; D013379:Substrate Specificity; D013696:Temperature
D003067:Coenzymes; D053138:Cyclohexenes; D004800:Enzymes, Immobilized; D011506:Proteins; C052985:isochorismic acid; D007535:Isomerases; D019751:Intramolecular Transferases; C058486:isochorismate synthase; D002827:Chorismic Acid; D008274:Magnesium