Abstract
A novel method to immobilize lipase on inorganic particles or on an inorganic porous plate is proposed. The method consists of entrapment of lipase into polyion complex, followed by fixation of the complex on the inorganic supports. It was simpler and offered much saving in time, comparing with conventional entrapping and covalently binding methods. Both the lipases immobilized on the particles and the plate showed high catalytic activity for esterification in organic medium, and the activity depended on kinds of polyion complex and water contents in the immobilized-lipases. The immobilized-lipases sustained their activity up to a significantly high temperature of 60° C, which suggests that lipase and polyion complex interact to enhance thermal stability of lipase. Activity holding with repeated uses was also studied.
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