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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.[1]

References

  1. Immobilization of isochorismate hydroxymutase. Comparison of native versus immobilized enzyme. Schaaf, P.M., Heide, L.E., Leistner, E.W., Tani, Y., el-Olemy, M.M. J. Nat. Prod. (1993) [Pubmed]
 
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