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Literature summary extracted from

  • Bolivar, J.M.; Wilson, L.; Ferrarotti, S.A.; Fernandez-Lafuente, R.; Guisan, J.M.; Mateo, C.
    Stabilization of a formate dehydrogenase by covalent immobilization on highly activated glyoxyl-agarose supports (2006), Biomacromolecules, 7, 669-673.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.17.1.9 biotechnology immobilization of enzyme on highly activated glyoxyl agarose, optimization protocol. Optimized enzyme retains 50% of the offered activity and becomes 50times more stable at high temperature and neutral pH. Optimal temperature increases by 10°C at pH 4.5. Immobilized enzyme accepts dextran-NAD+ as a substrate, use on ultra-filtration reactors to catalyze the recycling of NAD+ Pseudomonas sp.

General Stability

EC Number General Stability Organism
1.17.1.9 enzyme immobilized on highly activated glyoxyl agarose, retains full activity after 24 h in 50% acetone or dioxane. At 75% acetone, immobilized enzyme keeps more than 65% of initial activity after 4 days Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
1.17.1.9 Pseudomonas sp.
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.1.9 formate + dextran-NAD+ enzyme immobilized on glyoxyl agarose, 60% of the activity with NAD+ Pseudomonas sp. CO2 + dextran-NADH
-
 ?
1.17.1.9 formate + NAD+
-
 Pseudomonas sp. CO2 + NADH + H+
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.17.1.9 50
-
 native enzyme, pH 7.0, 10 h, fully active Pseudomonas sp.
1.17.1.9 63
-
 native enzyme, pH 7.0, half-life 1 h Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.1.9 NAD+
-
 Pseudomonas sp.