engleski

Optimization of enzymatic esterification of glycerol and oleic acid

Hydrolytic enzymes are the most commonly used biocatalysts in the organic synthesis. Esterase and lipase catalyze the hydrolysis and the formation of esters. Formally, lipase catalyzes the hydrolysis of lipids of fatty acids and glycerol at the lipid-water interface. Esterase and lipase have been used to catalyze synthetically useful reactions: ester hydrolysis, esterification (alcohol and acid), transesterification (alcohol and ester), interesterification (ester and acid) and the transfer of acyl groups from esters to other nucleophiles and hydroperoxide. These reactions often proceed stereoselectively in the aqueous-organic and organic solvents. The aim of the present work is to optimize the lipase catalyzed esterification of glycerol and oleic acid in the aqueous and the organic solvent, hexane, with lipase from Candida cylindracea (typical esterase). Generally, the initial reaction rates in the aqueous-organic systems are slower than the comparable reactions in the aqueous system, but the polarity nature of the organic solvent and the water content, influences the duration of the reaction and the conversion at the equilibrium. The water activity seems to be the limit rather than the water concentration. The esterification reactions were performed at 37 C, pH 6.0. The solvent (hexane) concentrations were varied.

optimization; enzymatic esterification; glycerol; olive oil

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