ABSTRACT
Several parameters related to the physicochemical state of the lipid substrate such as surface pressure and "interfacial quality", are known to affect the catalytic behavior of lipases in terms of both activity and selectivity (Rogalska et aL, 1993). This flexibility modulated by the reaction environment, together with the already mentioned variability observed in lipase proteins, provide researchers with a large - and to a considerable extent still unexploited - pool of candidate biocatalysts. As a consequence, a big deal of research is being devoted to the development of
lip~based reactions (see as a reference K. Drauz and H. Waldman, 1995). Some dozen of lipases are now commercially available; nevertheless those employed in large-scale industrial processes and products are still limited to a few cases, mainly due to the high price/low availability or non-optimal operational features of the naturally available enzymes. Therefore, perspectives in the use oflipases as industrial catalysts strongly rely on the production of recombinant enzymes with biochemical and catalytic features improved by protein engineering methods.
