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Production of citronellyl acetate in a fed-batch system using immobilized lipase

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Abstract

Several reports exist in the literature citing the decrease in conversion rates of organic-phase catalytic synthesis reactions when acetic acid is present as a reaction component. This inhibition is thought to result from damage to either the hydration layer-protein interaction or the overall enzyme structure. In this work, the inhibitory effect of acetic acid on lipase enzyme activity was ameliorated by conducting syntheses under acetic acid-limiting conditions in a fed-batch system, resulting in higher product yields. Periodic additions of acetic acid at levels of 40 mM or less gave maximum yields of 65% conversion for the reaction of citronellol and acetic acid to form citronellyl acetate. The enzyme used was a fungal lipase fromMucor miehei, and was immobilized on macroporous synthetic resin (a Novo lipozyme Novo Nordisk, Denmark). These results represent a fourfold improvement over batch runs reported in the literature for direct esterification of terpene alcohol with acetic acid using lipozyme as a catalytic agent.

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de Castro, H.F., Napoleão, D.A.S. & Oliveira, P.C. Production of citronellyl acetate in a fed-batch system using immobilized lipase. Appl Biochem Biotechnol 70, 667–675 (1998). https://doi.org/10.1007/BF02920178

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