High-rate membrane supported aqueous-phase enzymatic conversion in organic solvent.
Microporous membranes were used as a support material for enzyme immobilization by a supported aqueous-phase. To test the concept, a model reaction was chosen involving the oxidation of p-cresol by tyrosinase. Tyrosinase was first immobilized in a thin film of water formed on the inner surface of the membrane and then allowed to catalyze p-cresol oxidation in chloroform. By choosing optimal operating conditions, tyrosinase functioned catalytically for more than 6 hours with a stable reaction rate. The reaction rate was highly dependent on water content (water wt./enzyme wt. ratio) and permeation flux. Also, enzyme loading was an important factor for maintaining stable activity. This type of high-rate reactor utilized convective flow through an enzyme immobilized microporous membrane and provided high productivity by reducing mass transport limitations.
Yokoi
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Howard P. Isermann Department of Chemical Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180-3590.
Belfort
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D002725:Chloroform / Q000737:chemistry; D003408:Cresols / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000737:chemistry*; D008567:Membranes, Artificial; D014442:Monophenol Monooxygenase / Q000737:chemistry*; D010084:Oxidation-Reduction; D012997:Solvents; D013499:Surface Properties; D014867:Water
D003408:Cresols; D004800:Enzymes, Immobilized; D008567:Membranes, Artificial; D012997:Solvents; D014867:Water; C032538:4-cresol; D002725:Chloroform; D014442:Monophenol Monooxygenase