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Lipase is a potential biocatalyst and can be exploited for various applications such as food, pharmaceutical, oleochemistry, organic chemistry, biofuels and in detergent industries. In the present study, lipase from Aspergillus fumigatus was purified to homogeneity by SDS and Native PAGE and evaluated as biocatalyst for the synthesis of methyl butyrate which is a flavor ester. A purification fold of 6.96 was achieved by using Octyl Sepharose column chromatography. Methyl butyrate was synthesized by trans-esterification of vinyl butyrate with methanol, in a medium containing n-hexane as a solvent. The molar ratio of 2:2 (vinyl butyrate:methanol) was found to be optimum for the synthesis of methyl butyrate. The yield of methyl butyrate was maximum when reactants were incubated for 16 h at an incubation temperature of 40°C. The maximum yield (86%) of ester was obtained with 30 µg/ml of purified lipase.

Synthesis of Methyl Butyrate Catalyzed by Lipase from <i>Asper</i><i>gillus fumigatus</i>