Enzymatic synthesis using immobilized Enterococcus faecalis Esawy dextransucrase and some applied studies

Dextran and maltooligosaccharides (MOS) synthesis by immobilized Enterococcus faecalis Esawy dextransucrase, resulted in yielding of different Mw of applicable Dextran and MOS. They achieved a promising prebiotic and fibrinolytic activities. [Display omitted] •Dextrans and maltooligosaccharides was synthesis via immobilized dextransucrase.•Different parameters were studied for controlling dextrans and maltooligosaccharides MW.•Dextrans and MOS reported good prebiotic and fibrinolytic activities. Dextrans enzymatic synthesis by immobilized Enterococcus faecalis Esawy dextransucrase was studied. Different parameters, such as: enzyme protein concentration (EPC), substrate concentration (SC), temperature and reaction time were evaluated. EPC played a fundamental role in controlling dextran molecular size with 0.1% dextran in reaction mixture. Dextran 38,397 and 125,471Da were yielded at EPC 4.78 and 5.78mg, respectively. Proper dextrans (73,378 and 117,521Da) demanded in pharmaceutical applications were achieved at 6% and 12% sucrose concentrations and at 4.78 and 5.78mg EPC, respectively. Optimum temperature for conversion of glucose to dextran was 30°C (73% and 80% at 5.78 and 4.78mg EPC, respectively). Varieties of maltooligosaccharides (MOS) were yielded by synergistic cooperation between sucrose and maltose. Six MOS and three dextrans samples in vitro have prebiotic effect on Lactobacillus casei with degree of variation. Two samples of MOS with different degree of polymerization (DP) and three samples of dextran with different molecular weight (MW) reported different fibrinolytic activity.