LIPASE BIOCATALYSIS IN THE PRODUCTION OF ESTERS

Lipase biocatalysis was investigated as a tool for the production of butyl oleate and rapeseed oil 2-ethyl-1-hexyl ester by esterification and transesterification, respectively. We screened 25 commercially available lipases and found that butyl oleate was produced at high yields from oleic acid and 1-butanol by lipases from Candida rugosa, Chromobacterium viscosum, Rhizomucor miehei, and Pseudomonas fluorescens. The initial water content of the system, lipase quantity, and the molar ratio of l-butanol to oleic acid were important factors in influencing the ester yield In general, no ester was formed without the addition of water. The exception was Ch. viscosum lipase, which yielded 98% of ester in 12 h with 1-butanol excess without additional water. The addition of 3.2% water increased the initial rate of reaction. With an oleic acid excess and only 0.3% lipase, C. rugosa and R. miehei lipases yielded 94 and 100% esters with initial water contents of 3.2 and 14%, respectively. Lipase-catalyzed alcoholysis of low-erucic aci rapeseed oil and 2-ethyl-1-hexanol without additional organic solvent also was studied in stirred batch reactors. ln this case, C. rugosa lipase was the best biocatalyst with an optimal 2-ethyl-1-hexanol to rapeseed oil molar ratio of 2.8, a minimum of 1.0% added water, and 37 degrees C. An increase in temperature up to 55 degrees C increased the rate of reaction but did not affect the final ester yield. The enzyme was inactivated at 60 degrees C. Under optimal conditions the ester yield increased from 88% in 7 h to nearly complete conversion in 1 h when the lipase content was increased from 0.3 to 14.6%. ln a 2-kg small pilot scale, up to 90% conversion (97% of theoretical) was obtained in 8 h at 37 degrees C with 3.4% lipase in the presence of Amberlite XAD-7 resin with 3% added water.