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Literature summary for 3.2.1.26 extracted from

  • Raj, L.; Chauhan, G.S.; Azmi, W.; Ahn, J.H.; Manuel, J.
    Kinetics study of invertase covalently linked to a new functional nanogel (2011), Biores. Technol., 102, 2177-2184.
    View publication on PubMed
Search for more literature for 3.2.1.26

Application

Application Comment Organism
synthesis immobilization of invertase on a hydrogel comprised of methacrylic acid and N-vinyl pyrrolidone and ethyleneglycol dimethacrylate, converted to nanogel by an emulsification method and further functionalized by Curtius azide reaction. The values of Vmax, maximum reaction rate, of 0.123 unit/mg, Michaelis constant of 7.429 mol/L and energy of activation of 3.511 kJ/mol for the immobilized invertase are comparable with those of the free invertase at optimum conditions. The covalent immobilization enhances the pH and thermal stability of invertase Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.43
-
 sucrose immobilized enzyme, pH 6.0, 45°C Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
186
-
 immobilized enzyme, pH 6.0, 45°C Saccharomyces cerevisiae
218
-
 free enzyme, pH 6.0, 45°C Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose + H2O
-
 Saccharomyces cerevisiae beta-D-fructose + alpha-D-glucose
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
 free enzyme, rapid loss of activity above Saccharomyces cerevisiae
65
-
 immobilized enzyme, stable up to Saccharomyces cerevisiae

pH Range

pH Minimum pH Maximum Comment Organism
4 7.5 free enzyme Saccharomyces cerevisiae
4 9.5 immobilized enzyme Saccharomyces cerevisiae