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The lipase from Burkholderia cepacia, formerly known as Pseudomonas cepacia lipase, is a commercial enzyme in both soluble and immobilized forms widely recognized for its thermal resistance and tolerance to a large number of solvents and short-chain alcohols. The main applications of this lipase are in transesterification reactions and in the synthesis of drugs (because of the properties mentioned above). This review intends to show the features of this enzyme and some of the most relevant aspects of its use in different synthesis reactions. Also, different immobilization techniques together with the effect of various compounds on lipase activity are presented. This lipase shows important advantages over other lipases, especially in reaction media including solvents or reactions involving short-chain alcohols.

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The present work studies the sunflower oil hydrogenation on supported palladium catalysts, by analyzing the surface kinetics and the mass transfer limitations of products and reactants. Initially, a simplified model was studied. This model took into account only the consecutive hydrogenation of linoleic acid (diene), to reach the production of oleic (monoene) and stearic (saturated) acids. Using the adjusted values of the kinetic constants and the activation energies of the hydrogenation obtained with this model, a new scheme was investigated considering the geometric isomerization reactions (cis-trans). The diene hydrogenation constant was larger than that of the monoene. This fact confirms the higher reaction rate of the diene hydrogenation in comparison with that of the monoene. With respect to the isomerization rates, these have an activation energy superior to that of the monoene hydrogenation, and slightly superior to the diene hydrogenation activation energy. This fact verifies the influence of temperature on the formation of trans-isomers.

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