Immobilization of enzyme-encapsulated nanoporous material in a microreactor and reaction analysis

Abstract A microreactor containing lipase–nanoporous material composites was developed and employed in the hydrolysis reaction of a triglyceride. Lipase used as a model enzyme was encapsulated in two types of folded-sheet mesoporous silicas, FSM4 and FSM7, with pore diameters of approximately 4 and 7 nm, respectively. Direct microspectroscopic analysis of fluorescently labeled lipase immobilized in the FSM-containing microreactor revealed that the enzyme did not leach into the solution during the hydrolysis of the triglyceride, because of the stable immobilization of the enzyme. The lipase–FSM composites contained in the microreactor displayed higher enzymatic activity than those in a batch experiment. These results demonstrate that the enzyme microreactor using mesoporous silica was successfully constructed and that it exhibited high enzyme reactivities.

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