Add time:10/01/2019         Source:infona.pl

Lipolase 100 L, the lipase from the genetically engineered species of Aspergillus oryzae, has been used to catalyze esterification of lauric acid with aromatic alcohol-benzyl alcohol. A kinetic model for the lipase-catalyzed esterification in a biphasic organic-aqueous system has been proposed. Based on the interfacial substrate concentration, an analytical rate equation for initial rate of the reaction was derived and confirmed from the experimental data. The effect of various reaction parameters such as the speed of agitation, lipase concentration in the aqueous phase, aqueous phase volume, and reaction temperature on the progress of the esterification reaction using Lipolase 100 L have been studied. The initial reaction rate was found to be linearly dependant on the lipase concentration in the aqueous phase. The deactivating effect of benzyl alcohol at 40, 45 and 50 o C on Lipolase 100 L is also reported. Lipolase 100 L has also been used to catalyze esterification of lauric acid with phenyl ethyl alcohol. When fatty acids such as caprylic, capric, lauric and myristic acids were esterified with benzyl alcohol, the initial rate of reaction was found to be linearly proportional to the chain length of the fatty acid and lauric and myristic acids gave higher conversions. Aromatic acids as benzoic, phenyl acetic and cinnamic acids were not suitable substrates for this lipase for the esterification reaction.

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