Abstract
To develop excellent immobilized enzymes, monodisperse amphiphilic polymer particles that have both hydrophilic guanidino groups and hydrophobic acyl groups were synthesized and characterized. The monodisperse amphiphilic particles, which had an average diameter of 7.92 μm, had macropores with diameters ranging from 50 nm to 500 nm. The amount of Rhizopus delemar lipase immobilized on the monodisperse amphiphilic polymer particles was 150-8 700 times those of the immobilized lipases prepared by previous investigators using Dowex MWA-1, porous glass beads, and Sepharose 4B. The specific transesterification activity of the immobilized lipase prepared with the monodisperse amphiphilic polymer particles was 93.4 times that of the lyophilized lipase.
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