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- W1994080274 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 from Mucor 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." @default.
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- W1994080274 date "1998-01-01" @default.
- W1994080274 modified "2023-09-24" @default.
- W1994080274 title "Production of Citronellyl Acetate in a Fed-Batch System Using Immobilized Lipase Scientific Note" @default.
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- W1994080274 doi "https://doi.org/10.1007/978-1-4612-1814-2_61" @default.
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