Abstract

Novel polymeric macroporous hydrogels were developed to entrap and immobilize lipase. Poly(ethylene glycol) methyl ether acrylate hydrogel was used as the support. The emulsion-gelation method using oil-in-water emulsions was used to simultaneously synthesize the hydrogels and entrap lipase in the randomly distributed, non-interconnected, sphere-like macropores, which were several micrometers in diameter. The lipase, immobilized within the macroporous hydrogel, successfully catalyzed the hydrolysis of triacetin without leakage of lipase or loss of activity during repeated use. The macroporous hydrogel-immobilized lipase exhibited higher activity than the lipase immobilized within a non-porous hydrogel, which indicates entrapment of lipase in the macropores without interference from the polymer and excellent diffusional permeability of macroporous hydrogel to substrate/product species.

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