Enzymatic synthesis of oligosaccharides by recombinant Eschericia coli - expressed Candida molichiana β-glucosidase II

Abstract

In the present study, the biosynthetic activity of recombinant β-glucosidase from E. coli was described. The purified β-glucosidase from the recombinant E. coli – expressed C. molichiana (E. coli pBG₂₂: JM109) was obtained at the end of the fermentation process (24 h) with an enzyme activity of 180 IU/ml and the enzyme retained 93% of its initial activity in 20% (V/V) DMSO (dimethyl sulphoxide). The initial substrate concentration, the incubation time and temperature and the type of substrate was reported to influence the biosynthesis of oligosaccharides. The efficiency of the biosynthetic reaction increased to about 2-fold in the presence of DMSO. The yield of oligosaccharides was higher in the presence of sophorose than gentiobiose and cellobiose with DMSO.

Egyptian Journal of Biotechnology Vol. 25 (1) 2007: pp. 45-59