Investigation of keys parameters of fructose oleate enzymatic synthesis catalyzed by an immobilized lipase

The optimization of fructose fatty acid esters synthesis was performed by lipase-catalyzed transesterification. The experiments were carried out in a ternary alcohol, 2-methyl 2-butanol, using an immobilized Candida antartica lipase. A wide range of parameters was studied as enzyme concentration, stirring rate, temperature, stability and specificity of lipase. The obtained results indicated that the initial rate of reaction increases with the concentration of biocatalyst, the optimal stirring rate is about of 100 rpm. The chain length of the acyl donor (10-18 carbons) has not affected the performance of this synthesis. However, methanol, a byproduct has a strong inhibitor effect. The highest concentration (50 g l(-1)) and initial rate (90 g l(-1) h(-1)) were obtained at 90 degrees C. The stability of the enzyme was depended upon the temperature. At 60 degrees C, the biocatalyst has kept a high activity. At 80 degrees C, a drastic decrease of the initial rate was observed. (C) 1997 Elsevier Science B.V.