Enzyme Reaction in Organic Solvent. I.

Candida cylindracea Lipase Catalyzed Transesterification between Tri-n-butyrin and 1-Octanol in Various Organic Solvents

Abstract

The candida cylindracea lipase catalyzed transesterification between tri-n-butyrin (1) and 1-octanol (2) to give 1-octyl butyrate (3) was studied in various organic solvents containing 0.75M of (1) and 0.67M of (2) at 30°C. The rate of this reaction increased at first, through a maximum and then decreased with increasing water content. The water content at the maximum rate, (H₂O) _op, for the reaction in a water-insoluble solvent increased with enzyme concentration. (H₂O) _op was invariable and independent of enzyme concentration for the reaction in water-soluble solvents. The rate in the presence of (H₂O) _op was measured and transesterification was found to be predominated by the structure and polarity of the solvent.