Improved production of butyl butyrate with lipase from Thermomyces lanuginosus immobilized on styrene-divinylbenzene beads

Two immobilized preparations from Thermomyces lanuginosus lipase (TLL) were compared in the synthesis of butyl butyrate. The commercial Lipozyme TL-IM, and TLL immobilized on styrene–divinylbenzene beads (MCI-TLL) were tested in the esterification reaction using n-hexane as solvent. The variables temperature (30–60 °C), substrate molar ratio (1:1 to 5:1), added water (0–1%), and biocatalyst content (3–40%) were evaluated in terms of initial reaction rate for each biocatalyst. SDS–PAGE analysis revealed that MCI-TLL had an immobilized enzymatic load twice as high as Lipozyme TL-IM, but with an activity 3-fold higher. MCI-TLL presented high initial reaction rates up to 1.0 M butyric acid, while Lipozyme TL-IM showed a decrease in its activity above 0.5 M. Moreover, MCI-TLL allowed a productivity of 14.5 mmol g−1 h−1, while Lipozyme TL-IM 3.2 mmol g−1 h−1, both by mass of biocatalyst.This work was supported by grants from FAPERGS – ARD/2011, from CNPq – Universal/2011, both from Brazil, and CTQ2009-07568 from Spanish Ministerio de Ciencia e Innovación. The authors wish to thank Mr. Ramiro Martínez (Novozymes, Spain) for kindly supplying the enzymes used in this research. We also thank Ministerio de Ciencia e Innovación (Spain) for a fellowship for C. Garcia-Galan, the PhD Program Fellowship-2008 from COLCIENCIAS (Colombia) for a fellowship for O. Barbosa, CNPq (Brazil) for a fellowship to J. L. R. Friedrich, and FAPERGS (Brazil) for a fellowship to A. B. Martins.Peer Reviewe