Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10160639 | Biochemical Engineering Journal | 2005 | 9 Pages |
Abstract
Experimental data reported in this manuscript do not belong to equilibrium data but to enzymatic activity attained in the first 2 h of reaction. After this period, it was shown that, in the current synthesis, deactivation/agglomeration/inhibition of the catalyst prevented further CRL activity. However, 2 h measurements allowed fulfilling the aim of this work: the determination of the best conditions for ethyl oleate production in short periods of time, using an immobilised derivative of a relatively cheap lipase as it is C. rugosa lipase. Best results were achieved in the reaction performed at 45 °C and 350 rpm, with an initial stoichiometric ratio of substrates, 20% of aqueous content, and mediated by 50 mg of CR/PP (0.0585 mmol/mg of CR-h). The deleterious effect of ethanol excess and agglomeration of the native and immobilised catalyst have been analysed.
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Authors
M.L. Foresti, A. Errazu, M.L. Ferreira,