The production of the Bacillus subtilis /3-glucanase enzyme was examined in the yeast Saccharomyces cerevisiae. The ability of the bacterial signal peptide to translocate and secrete the enzyme was analysed and compared to the yeast a-factor signal peptide. A truncated version of the signal was also examined as was the effect of complete removal of the signal sequence. Glycosylation of the /3-glucanase enzyme in the yeast secretory pathway was examined using both Western blots and activity gels and the effects of glycosylation on /3-glucanase production was assessed. A second bacterial enzyme, /3-glucuronidase, was also examined for its potential use as a reporter enzyme in yeast expression and secretion systems. This work included attempts to secrete the enzyme, the definition of its active site, investigation of its potential for use in translational fusion experiments and the generation of a polyclonal antibody to the E.coli /3-glucuronidase enzyme.