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Literature summary for 3.2.1.3 extracted from

  • Gottschalk, N.; Jaenicke, R.
    Authenticity and reconstitution of immobilized enzymes: characterization and denaturation/renaturation of glucoamylase II (1991), Biotechnol. Appl. Biochem., 14, 324-335.
    View publication on PubMed
Search for more literature for 3.2.1.3

General Stability

General Stability Organism
denaturation and renaturation does not seem to offer an economical approach to improve the usage time of immobilized enzyme Aspergillus niger

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.13
-
 maltopentaose free enzyme Aspergillus niger
0.15
-
 maltoheptaose immobilized enzyme Aspergillus niger

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
 glucoamylase II
-

Renatured (Commentary)

Renatured (Comment) Organism
optimal renaturation Aspergillus niger

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Aspergillus niger

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
maltoheptaose + H2O
-
 Aspergillus niger ?
-
 ?
maltopentaose + H2O
-
 Aspergillus niger ?
-
 ?
starch + H2O
-
 Aspergillus niger glucose + ?
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 pH 4.5, 5 min, stable up to Aspergillus niger

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
-
 free and immobilized enzyme Aspergillus niger

pH Range

pH Minimum pH Maximum Comment Organism
2 7 pH 2.0: about 55% of maximal activity, pH 7.0: about 25% of maximal activity, free and immobilized enzyme Aspergillus niger