ABSTRACT
Candida rugosa (formerly Candida cylindracea) lipase (CRL) is a very important industrial enzyme widely used in biotechnological applications such as the production of fatty acid, the synthesis of various esters, and the resolution of racemic mixtures.1-7 However, crude enzyme preparations obtained from the various commercial suppliers exhibit remarkable variation in their catalytic efficiency and stereospecificity.8 Seven lipase genes, namely LIP1 to LIP7, have been described in C. rugosa. However, only three lipases (LIP1, LIP2, and LIP3) have been identified9-13 in commercial crude enzyme preparations. The purified isoenzymes displayed different substrate specificities and thermal stabilities.10,12,14-16 Native CRLs produced by a conventional fermentation process contain variable mixtures of isoforms due to the differential responses of different genes of CRL isoforms in wild type and mutant strains to fermentation conditions.17,18 This results in serious problems in biotechnological applications due to the irreproducibility brought about by using enzymes from various suppliers, or even different batches, and the complications in interpretations.
