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Enzymic Interesterification of fats: Immobilization and Immunogold Localization of Lipase on Ion-Exchange Resins

1990; Taylor & Francis; Volume: 3; Issue: 4 Linguagem: Inglês

10.3109/10242429008992076

0886-4454

A. P. Ison, P. Dunnill, M. D. Lilly, Alasdair R. Macrae, Colin Smith,

Enzyme Catalysis and Immobilization

A 1,3 specific lipase from Mucor miehei has been immobilized to two phenolformaldehyde resins with active tertiary amine groups and different porous structures (Duolite ES562 and ES568N). Duolite ES568N has a more uniform pore structure, allowing more rapid uptake of lipase. Immobilized lipase particles were treated by washing, dehydration with glycolmethacrylate and embedding in polymer. Following immunogold staining of thin sections, examined by electron or light microscopy showed that the location of the lipase was dependent on the pore structure of the support material and the immobilization time.