Covalent immobilization of Enterococcus faecalis Esawy dextransucrase and dextran synthesis

Enterococcus faecalis Esawy dextransucrase was immobilized in Fe3+-cross-linked alginate/carboxymethyl cellulose (AC) beads. The gel beads were modified with polyethylenimine (PEI) followed by glutaraldehyde (GA) to form Fe3+ (ACPG) beads. Fe3+ (ACPG) was characterized using FTIR and DSC techniques....

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Bibliographic Details
Published inInternational journal of biological macromolecules Vol. 82; pp. 905 - 912
Main Authors Hashem, Amal M., Gamal, Amira A., Hassan, Mohamed E., Hassanein, Naziha M., Esawy, Mona A.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.01.2016
Subjects
Covalent binding
Dextran
Dextrans - chemical synthesis
Dextrans - chemistry
Dextransucrase
Enterococcus faecalis
Enterococcus faecalis - enzymology
Enterococcus faecalis - isolation & purification
Enzyme Stability
Enzymes, Immobilized - chemistry
Enzymes, Immobilized - metabolism
Glucosyltransferases - chemistry
Glucosyltransferases - metabolism
Hydrogen-Ion Concentration
Immobilization
Kinetics
Microspheres
Oligosaccharides
Spectroscopy, Fourier Transform Infrared
Temperature
Thermodynamics
Dextran
Enterococcus faecalis
Immobilization
Dextransucrase
Covalent binding
Oligosaccharides
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Summary:Enterococcus faecalis Esawy dextransucrase was immobilized in Fe3+-cross-linked alginate/carboxymethyl cellulose (AC) beads. The gel beads were modified with polyethylenimine (PEI) followed by glutaraldehyde (GA) to form Fe3+ (ACPG) beads. Fe3+ (ACPG) was characterized using FTIR and DSC techniques. GA activated beads showed new two peaks. The first was at 1717cm−1 which refers to (CO) group of a free aldehyde end of glutaraldehyde, and another peak was at 1660cm−1 referring to (CN) group. The immobilization process improved the optimum temperature from 35 to 45°C. The immobilized enzyme showed its optimum activity in wide pH range (4.5–5.4) compared to pH 5.4 in case of free form. Also, the immobilization process improved the thermal and pH enzyme stability to great extent. Reusability test proved that the enzyme activity retained 60% after 15 batch reactions. Immobilized enzyme was applied successfully in the synthesis of oligosaccharides and different molecular weights of dextran.
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ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2015.09.076