STEREOCHEMICAL PURIFICATION OF AN ANTI-INFLAMMATORY DRUG IN AN ENZYME MEMBRANE REACTOR

ENZYMATIC RESOLUTION IS A POTENTIALLY POWERFUL APPROACH TO THE SEPARATION OF STEREOISOMERS, AND LIPASES AND CARBOXYLESTERASES ARE AMONG THE MORE ATTRACTIVE AND EXTENSIVELY STUDIED ENZYMES FOR THIS PURPOSE. MANY LIPASE SUBSTRATES -- AND MANY COMPLEX MOLECULES WITH CHIRAL CENTERS -- ARE POORLY SOLUBLE IN WATER, HOWEVER, AND THUS THESE BIOCONVERSIONS MUST OFTEN BE PERFORMED IN MULTIPHASE, EMULSION-TYPE ENZYME REACTORS WHERE THREE PHASES ARE SIMULTANEOUSLY PRESENT: ORGANIC, AQUEOUS, AND IMMOBILIZED ENZYME. UNFORTUNATELY, THESE SYSTEMS HAVE SEVERAL PROCESS ENGINEERING LIMITATIONS. MULTIPHASE AND EXTRACTIVE MEMBRANE BIOREACTORS BASED ON NOVEL HOLLOW-FIBER MODULES OFFER SEVERAL ADVANTAGES IN MULTIPHASE BIOCHEMICAL CONVERSIONS. IN PARTICULAR, THEY PROMOTE EFFICIENT INTRAPHASE MASS TRANSFER, THEY AVOID DISPERSING ONE IMMISCIBLE PHASE WITHIN ANOTHER, AND THEY SEPARATE REACTION PRODUCTS AS THEY ARE FORMED. IN PHASE I, THE TECHNICAL AND ECONOMIC FEASIBILITY OF MULTIPHASE AND EXTRACTIVE MEMBRANE BIOREACTOR PROCESSES FOR THE ENZYME-MEDIATED RESOLUTION OF THE POTENT AND THE INACTIVE ISOMERIC FORMS OF A SUBSTANTIALLY WATER-INSOLUBLE ANTI-INFLAMMATORY PHARMACEUTICAL IS EXAMINED. THE KEY ENZYME PARAMETERS OF ACTIVITY AND STEREOSELECTIVITY WILL BE MEASURED, A PROTOTYPE ENZYME MEMBRANE REACTOR WILL BE OPERATED, AND ITS PERFORMANCE WILL BE EVALUATED.