Secretion of Bacillus endoglucanase in Saccharomyces cerevisiae by its own signal sequence

Abstract

To examine whether the signal sequence of Bacillus endo-1, 4-glucanase can act functionally in a yeast, a lower eucaryote, two recombinant plasmids were constructed and introduced into Saccharomyces cerevisiae: recombinant plasmid pGCMC10 containing the complete signal sequence of Bacillus endoglucanase, and pGCMC11 without the signal sequence. Secretion of endoglucanase into culture medium was obtained with the yeast transformant containing plasmid pGCMC10. The secreted endoglucanase was glycosylated and was apparently processed to be about 36 kilodaltons (KDa) and 43KDa proteins. The glycosylated endoglucanase from yeast transformant was more thermostable than the nonglycosylated endoglucanase from Escherichia coli transformant.