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Enzymatic synthesis of esters using an immobilized lipase

1991; Wiley; Volume: 37; Issue: 11 Linguagem: Inglês

10.1002/bit.260371104

1097-0290

Giorgio Carta, John L. Gainer, Alan H. Benton,

Microbial Metabolic Engineering and Bioproduction

Abstract Various esters were synthesized in nearly anhydrous hexane from alcohols and carboxylic acids using a lipase from Candida cylindracea . The enzyme was immobilized on a nylon support and protein loadings as high as 10 mg/g were obtained. The activity of the immobilized enzyme was maximum in a range of temperatures from 25 to 37°C. Ethylpropionate was formed from ethanol and propionic acid at a rate of 0.017 mol/h g immobilized protein. Different esters were formed at comparable rates and equilibrium conversions could generally be approached in less than 10 h in a batch reaction system. The immobilized lipase catalyst was quite stable and retained about one third of the initial activity after repeated experiments during the course of 72 days. A stirred tank continuous flow reactor was used successfully for the continuous production of esters.