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

Area of Science:

• Biotechnology
• Enzymology
• Carbohydrate Chemistry

Background:

• Dextransucrase from Enterococcus faecalis is a key enzyme for dextran synthesis.
• Controlling dextran molecular weight is crucial for pharmaceutical applications.
• Enzyme immobilization enhances enzyme stability and reusability.

Purpose of the Study:

• To investigate the enzymatic synthesis of dextrans using immobilized Enterococcus faecalis dextransucrase.
• To evaluate the impact of enzyme protein concentration (EPC), substrate concentration (SC), temperature, and reaction time on dextran production.
• To characterize dextrans produced for potential pharmaceutical and prebiotic applications.

Main Methods:

• Enzymatic synthesis of dextrans using immobilized Enterococcus faecalis dextransucrase.
• Optimization of reaction parameters including enzyme protein concentration, sucrose concentration, and temperature.
• Characterization of synthesized dextrans by molecular weight (MW) and degree of polymerization (DP).
• In vitro assessment of prebiotic effects on Lactobacillus casei and fibrinolytic activity.

Main Results:

• Enzyme protein concentration significantly influenced dextran molecular size, yielding specific MWs at different EPCs.
• Optimal dextran yields for pharmaceutical applications were achieved at specific sucrose concentrations and EPCs.
• Optimum temperature for dextran synthesis was determined to be 30°C.
• Maltooligosaccharides (MOS) were produced, and both MOS and dextran samples exhibited prebiotic effects and fibrinolytic activity.

Conclusions:

• Immobilized Enterococcus faecalis dextransucrase offers a controllable method for synthesizing dextrans with specific molecular weights.
• The synthesized dextrans and MOS possess potential for pharmaceutical and prebiotic applications.
• Further research can explore the structure-activity relationships of these dextrans and MOS.