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Lipase-catalyzed synthesis of isoamyl butyrate: Optimization by response surface methodology

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Journal of the American Oil Chemists' Society

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Abstract

Immobilized lipase from Mucor miehei (Lipozyme IM-20) was employed in the esterification of butyric acid and isoamyl alcohol to synthesize isoamyl butyrate in n-hexane. Response surface methodology based on five-level, five-variable central composite rotatable design was used to evaluate the effects of important variables—enzyme/substrate (E/S) ratio (5–25 g/mol), acid concentration (0.2–1.0 M), alcohol concentration (0.25–1.25 M), incubation period (12–60 h), and temperature (30–50°C)—on esterification yield of isoamyl butyrate. In the range of parameters studied, the extent of esterification decreased with temperature, lower E/S ratios, and incubation periods. Excess acid and alcohol concentrations (i.e., acid/alcohol >1.4 or alcohol/acid >1.4) were found to decrease yield probably owing to inhibition of the enzyme by acid or alcohol, the former being more severe. The optimal conditions achieved are as follows: E/S ratio, 17 g/mol; acid concentration, 1.0 M; incubation period, 60 h; alcohol concentration, 1.25 M; and temperature, 30°C. With these conditions, the predicted value was 1.0 M ester, and the actual experimental value was 0.98 M.

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Correspondence to N. G. Karanth.

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Krishna, S.H., Manohar, B., Divakar, S. et al. Lipase-catalyzed synthesis of isoamyl butyrate: Optimization by response surface methodology. J Amer Oil Chem Soc 76, 1483–1488 (1999). https://doi.org/10.1007/s11746-999-0189-x

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  • DOI: https://doi.org/10.1007/s11746-999-0189-x

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