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Literature summary for 3.2.1.11 extracted from

  • Hashem, A.M.; Gamal, A.A.; Hassan, M.E.; Hassanein, N.M.; Esawy, M.A.
    Covalent immobilization of Enterococcus faecalis Esawy dextransucrase and dextran synthesis (2016), Int. J. Biol. Macromol., 82, 905-912.
    View publication on PubMed

Application

Application Comment Organism
synthesis immobilization of enzyme in Fe3+-cross-linked alginate/carboxymethyl cellulose beads. The immobilization process improves the optimum temperature from 35°C to 45°C. The immobilized enzyme shows its optimum activity for synthesis of dextran in pH range 4.5-5.4 compared to pH 5.4 in case of free form. The immobilization process improve the thermal and pH enzyme stability to great extent. The enzyme retains 60% activity after 15 batch reactions Enterococcus faecalis

Organism

Organism UniProt Comment Textmining
Enterococcus faecalis
-
Esawy
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose
-
Enterococcus faecalis oligosaccharides + dextran + H2O
-
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Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
native enzyme Enterococcus faecalis
45
-
immobilized enzyme Enterococcus faecalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5 5.4 immobilized enzyme Enterococcus faecalis
5.4
-
native enzyme Enterococcus faecalis