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Ability of Vasconcellea x heilbornii lipase to catalyse the synthesis of alkyl esters from vegetable oils

Cambon E., Bourlieu C., Chan Salum T.F., Piombo G., Dubreucq E., Villeneuve P.. 2009. Process Biochemistry (1991), 44 (11) : p. 1265-1269.

DOI: 10.1016/j.procbio.2009.07.003

Lipase-catalysed synthesis of alkyl esters is regarded as a potential alternative to chemical catalysis. Owing to its availability as a waste material from the babaco fruit production, its strong lipolytic activity and its natural immobilization, the dried latex of Vasconcellea x heilbornii appears as a good candidate to produce alkyl esters. The ability and performance of this lipase to catalyse the alcoholysis of sunflower oil with various primary alcohols was evaluated in a solvent-free system. A linear correlation between the final reaction rate and the alcohol polarity was established. For methanolysis, the influence of substrates ratio on final conversion rate was studied at different temperatures. At 30°C, the lipase was inactivated by shaking in a mixture containing more than 0.5 molar equivalents of methanol; the minimum methanol concentration for enzyme deactivation increased with temperature. Moreover, for a 0.5:1 methanol/TAG molar ratio, conversion rates of 73, 66 and 55% were obtained at 30, 40 and 55°C respectively, showing that the increase of temperature diminished the final methanolysis conversion rate. These facts were associated to the miscibility of methanol in oil and to the thermodynamic state of the medium. To overcome the inactivation of the lipase by methanol, alcoholysis was carried out by fractionated addition of methanol. In those conditions, Vasconcellea heilbornii latex could catalyse the conversion of 70% of sunflower TAGs in methyl esters at 30°C.

Mots-clés : huile de tournesol; caricaceae; latex; biocatalyseur; estérase; estérification; alcool; ester; catalyse; lipase; vasconcellea; alcoolyse

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