Synthesis of monocaprin catalyzed by lipase.

Marco A M Da Silva, Vitória C Medeiros, Marta A P Langone, Denise M G Freire

Index: Appl. Biochem. Biotechnol. 105 -108 , 757-67, (2003)

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Abstract

The production of monoglyceride emulsifiers commonly employed in the food, cosmetic, and pharmaceutical industries can be catalyzed by lipases, biocatalysts that are becoming increasingly attractive in the enzyme market. The aim of this study was to produce monocaprin utilizing a commercial immobilized lipase (Lipozyme IM 20) through the direct esterification of capric acid and glycerol. Experiments were performed for 6 h in an open reactor and the products were analyzed by gas chromatography. The parameters investigated were the amount of enzyme, temperature, and molar ratio between the reagents (capric acid/glycerol). The experimental runs followed an experimental design generated using Statistica software. The results showed that all the parameters were significant and that monocaprin production was enhanced at the lower ranges of the tested variables. The best conditions established were 55 degrees C, 3% (w/w) enzyme concentration, and molar ratio of 1. The final product, obtained after 6 h of reaction, was 61.3% monocaprin, 19.9% dicaprin, and 18.8% capric acid. This composition satisfies the directives of the World Health Organization food emulsifiers, which requires that these mixtures have at least 70% mono- plus diglyceride, and a minimum of 30% monoacylglycerol.