Lipase-catalyzed transesterification of rapeseed oil and 2-ethyl-1-hexanol

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[1] Linko, Y.-Y.
[2] Lamsa, M.
[3] Huhtala, A.
[4] Linko, P.
来源
Linko, Y.-Y. | 1600年 / American Oil Chemists' Soc, Champaign, IL, United States卷 / 71期
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Alcohols - Bioconversion - Catalyst deactivation - Chemical reactors - Enzymes - Esterification;
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摘要
Lipase-catalyzed transesterification (alcoholysis) of low-erucic acid rapeseed oil and 2-ethyl-1-hexanol without an additional organic solvent was studied in stirred batch reactors. Of a number of commercially available enzymes investigated, the best results were obtained with a Candida rugosa lipase. The optimal transesterification conditions were an oil/alcohol molar ratio of 1:2.8, a minimum of 1.0% (w/w) added water, and with a temperature of 37-55 °C. Under the optimal conditions, a nearly complete conversion was obtained in one hour with 14.6% (w/w) lipase, whereas 0.3% (w/w) lipase required 10 h for similar results. The enzyme was inactivated at 60 °C.
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