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Literature summary for 2.4.1.5 extracted from

  • Gomez de Segura, A.; Alcalde, M.; Yates, M.; Rojas-Cervantes, M.L.; Lopez-Cortes, N.; Ballesteros, A.; Plou, F.J.
    Immobilization of dextransucrase from Leuconostoc mesenteroides NRRL B-512F on Eupergit C supports (2004), Biotechnol. Prog., 20, 1414-1420.
    View publication on PubMed

General Stability

General Stability Organism
native enzyme loses 90% of its inital activity in only 2 h at pH 5.4, 30°C, immobilization on Eupergit C 250L significantly stabilizes dextransucrase. Despite a fast partial inactivation in the first 2 h, the enzyme immobilized on Eupergit C 250L maintains more than 40% of the initial activity over the following 2 days, the enzyme immobilized on Eupergit C maintains about 15% of the initial activity after 1 day Leuconostoc mesenteroides

Organism

Organism UniProt Comment Textmining
Leuconostoc mesenteroides
-
NRRL B-512F
-
Leuconostoc mesenteroides NRRL B-512F
-
NRRL B-512F
-

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30
-
pH 5.4, native enzyme loses 90% of its inital activity in only 2 h, immobilization on Eupergit C 250L significantly stabilizes dextransucrase. Despite a fast partial inactivation in the first 2 h, the enzyme immobilized on Eupergit C 250L maintains more than 40% of the initial activity over the following 2 days, the enzyme immobilized on Eupergit C maintains about 15% of the initial activity after 1 day Leuconostoc mesenteroides

pH Stability

pH Stability pH Stability Maximum Comment Organism
5.4
-
30°C, native enzyme loses 90% of its inital activity in only 2 h Leuconostoc mesenteroides