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Literature summary 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

General Stability

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.3 0.13
-
 maltopentaose free enzyme Aspergillus niger
3.2.1.3 0.15
-
 maltoheptaose immobilized enzyme Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.3 Aspergillus niger
-
 glucoamylase II
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.2.1.3 optimal renaturation Aspergillus niger

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.3 60
-
 pH 4.5, 5 min, stable up to Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.3 4.5
-
 free and immobilized enzyme Aspergillus niger

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.3 2 7 pH 2.0: about 55% of maximal activity, pH 7.0: about 25% of maximal activity, free and immobilized enzyme Aspergillus niger