Fusion between serine-threonine reach domain from STA1 gene with BGLB gene of the Paenibacillus polymyxa

Abstract

Beta-glucosidase gene of bacterian origin was cloned in Saccharomyces cerevisiae to enable growth on disaccharide, cellobiose. To promote the secretion of ß-glucosidase B, the catalitic domain of bglB gene was fused with the serinethreonine rich domain of the STA1 gene and was inserted into an yeast expression vector under control of the CYCGAL inductible S. cerevisiae promoter. Expression of hybrid gene and proteine secretion was verified in Saccharomyces cerevisiae with p-nitrophenyl-ß-D-glucopyranoside as substrate.
Genetically stable and regulated expression in Saccharomyces cerevisiae of ß-glucosidase activity is interesting for the development of strains able to ferment ß-glycosidic sugars (i.e. cellobiose and lactose).