Properties of free and immobilised lipase from Burkholderia cepacia in organic media

The purified lipase from Burkholderia cepacia was immobilised on a porous p olypropylene support and its biocatalytic properties were compared with tho se of the free enzyme in organic media. For both lipase preparations, the r ate of p-nitrophenyl eater hydrolysis in n-heptane was not restricted by ma ss transfer limitations. The immobilisation changed neither the temperature at which the reaction rate was maximal, nor the activation energy of the r eaction. The enzyme stability was slightly decreased (1.3-fold) upon immobi lisation. Moreover, the immobilised enzyme displayed fewer variations df ac tivity with fatty acid chain length. Interestingly, for all the different p -nitrophenyl esters used, the immobilised enzyme was more active (from 5.8- to 18.9-fold) than the free enzyme. Therefore, it would be very useful to use B. cepacia lipase immobilised onto porous polypropylene for application s in organic media, as it displayed high activities on a larger range of su bstrates.