COMPARISON OF LIPASES FROM DIFFERENT STRAINS OF THE FUNGUS GEOTRICHUM-CANDIDUM

The type A lipase and the cis-9 18:1 specific type B lipase of differe nt strains of Geotrichum candidum were compared. Comparing the enzyme activity of crude lipase preparation and purified type A and type B li pases and the protein pattern of these preparations in denaturing poly acrylamide gel electrophoresis (SDS-PAGE) revealed that the specific a ctivity for cis-9 18:1 fatty acids was related to the content of the t ype B lipase. Tandem-crossed immunoelectrophoresis was used to demonst rate immunological identity between type A and type B lipase of G. can didum ATCC 66599. Partial immunological identity was observed between type B lipase of this strain and type A lipase of G. candidum ATCC 346 14 and two commercial crude G. candidum lipase preparations (Amano and Biocatalyst), i.e., the type B lipase of G. candidum ATCC 66592 had i mmunogenic epitopes which are not present on the other lipases. Enzyma tic deglycosylation of the lipases did not alter this pattern. After p artial proteolysis of purified type A and type B lipases of G. candidu m ATCC 66592, Amano and Biocatalyst, no difference between the type A lipase of the three strains was observed in SDS-PAGE. For all strains the type B lipase exhibited a distinctly different peptide pattern to that of the type A lipase. In addition, the type B lipase of G. candid um ATCC 65592 differed from the type B lipase of Amano and Biocatalyst by having an additional peptide band. The results indicate that the G . candidum ATCC 66592 should be considered a distinct strain regarding the protein chemical characteristics of its type B lipase, whereas th e two commercial lipase preparations appear to be very similar.