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Literature summary for 3.2.1.26 extracted from

  • Arruda, L.M.O.; Vitolo, M.
    Characterization of invertase entrapped into calcium alginate beads (1999), Appl. Biochem. Biotechnol., 81, 23-33.
    View publication on PubMed
Search for more literature for 3.2.1.26

Application

Application Comment Organism
nutrition enzymatic sucrose hydrolysis with invertase entrapped into calcium alginate beads is more attractive for industrial use than the acid hydrolysis process Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.2
-
 sucrose invertase entrapped into calcium alginate beads Saccharomyces cerevisiae
41.2
-
 sucrose free enzyme Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
 above, enzyme entraped into calcium alginate beads is more stable than the soluble one Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.6
-
 free enzyme and enzyme entrapped into calcium alginate beads Saccharomyces cerevisiae

pH Stability

pH Stability pH Stability Maximum Comment Organism
2.8 8 soluble enzyme is stable over the overall pH interval, the enzyme entrapped into calcium alginate beads loses 34% of its original activity as the pH varies from 3.0 to 4.6, but at pH-values above 4.6 the residual activity remains unchanged. At pH 8.0 the entrapped invertase is stable for at least 30 h Saccharomyces cerevisiae