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Literature summary extracted from

  • Arica, M.Y.; Alaeddinoglu, N.G.; Hasirci, V.
    Immobilization of glucoamylase onto activated pHEMA/EGDMA microspheres: properties and application to a packed-bed reactor (1998), Enzyme Microb. Technol., 22, 152-157.
No PubMed abstract available

Application

EC Number Application Comment Organism
3.2.1.3 synthesis the immobilized enzyme with high operational stability can be used for continuous production of glucose from soluble dextrin Aspergillus niger

General Stability

EC Number General Stability Organism
3.2.1.3 high operational stability of the enzyme immobilized onto poly(2-hydroxyethyl methacrylate)/ethylene glycol dimetharylate microspheres Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.3 0.17
-
Dextrin free enzyme Aspergillus niger
3.2.1.3 0.83
-
Dextrin immobilized enzyme Aspergillus niger
3.2.1.3 6.2
-
maltose free enzyme Aspergillus niger
3.2.1.3 27.4
-
maltose immobilized enzyme Aspergillus niger

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.3 dextrin + H2O
-
Aspergillus niger ?
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.3 50
-
free enzyme Aspergillus niger
3.2.1.3 55
-
immobilized enzyme Aspergillus niger

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.3 30 60 30°C: about 30% of maximal activity, immobilized enzyme, 30°C: about 50% of maximal activity, free enzyme, 60°C: about 50% of maximal activity, free enzyme, 60°C: about 90% of maximal activity, immobilized enzyme Aspergillus niger

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.3 additional information
-
thermostability of immobilized glucoamylase increases considerably as a result of covalent immobilization onto poly(2-hydroxyethyl methacrylate)/ethylene glycol dimetharylate microspheres Aspergillus niger
3.2.1.3 70
-
250 min, immobilized enzyme loses 60% of its activity, half-life: 220 min. Free enzyme loses 75% of its activity, half-life 140 min Aspergillus niger

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.3 2.5 8 pH 2.5: about 35% of maximal activity, immobilized enzyme, pH 2.5: about 55% of maximal activity, free enzyme, pH 8.0: about 25% of maximal activity, free enzyme, pH 8.0: about 50% of maximal activity, immobilized enzyme Aspergillus niger