The major drawbacks of native lipase applications in processes occurring in water or in organic solvents include: difficulties in catalyst recycling, low activity and operational instability. The immobilization of Burkholderia cepacia lipase by adsorption or covalent binding onto 5 differently functionalized carriers (silica, acrylic, cellulose-based) was performed to overcome this problem. The optimization of the reaction preparation in water-rich media was based on the hydrolytic reactivity of the preparations, as well as the thermal, operational and storage stabilities. Aminated silica carrier, activated with glutaraldehyde, was determined to be the carrier of choice. Regarding processes in water-restricted media, carrier selection was based on reactivity after drying and five preparations were chosen for the resolution of a non-equimolar isomer mixture (85:15 ratio of R to S isomers), treating the kinetic resolution of ((+)-(S/R)-1-[(1S,5R)-6,6-dimethylbicyclo[3.1.0]hex-2-en-2-yl)]ethanol as a model. The resulting acetate of R configuration exhibits interesting sensory properties. The operational stability of the chosen catalysts was tested over 15 consecutive batch processes; the most beneficial results were obtained with lipase adsorbed on an acrylic carrier. Conversion increased gradually from 10 to 84% over the first five processes, which could be explained by the product sorption onto the carrier. Full kinetic resolution with maximal substrate conversion (approximately 84%) was achieved and remained stable during the next 10 runs, an excellent result, and thus, the proposed system might be regarded as an exceptionally attractive solution for the perfume and cosmetic industries.
Keywords: Batch reactor; Biocatalysis; Burkholderia cepacia lipase (BCL); Immobilization; Kinetic resolution.
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