Lipases are versatile and selective enzymes, stable in organic media, which catalyze hydrolysis, esterification and transesterification reactions. Esterification reactions with fatty acids and carbohydrates or short-chain alcohols result on produdcts with great commercial interest, i.e. fatty esters of sugars (biosurfactants) or aromas, respectively. The combination of cyclodextrines (CDs, cyclic molecules formed by the junction of 6, 7 or 8 glucose molecules) with fatty acids might change the permeability of drugs through the skin, probably because of interaction with lipids. The great problem with the enzymatic production of biosurfactants by esterification between sugars and fatty acids in organic media is the solubilization of the sugar. An alternative to the organic solvent would be the use of ionic liquids, which have a low vapor pressure and are considered a "green" solvent. The usage of enzymes on a soluble form is not economically attractive, due to its high production costs and operational frailty. An alternative to surpass these inconveniences is the enzyme immobilization on solid supports, rendering stable and insoluble catalysts. Nowadays much has been studied about the immobilization of enzymes on magnetic support, which permits a highly selective recuperation of the derivatives by applying an external magnetic field. The use of immobilized enzymes enables a continuous process with different reactor configuration, the east control and interruption of the reaction. In this context, it is intended on this project the study of the enzymatic synthesis of long-chain esters (sugar esters) and short-chain esters (aromas), in the presence of ionic liquids, evaluating the production on a batch reactor (conventional and microwave-assisted) and on an continuous one (in fixed and/or fluidized bed).
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