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Literature summary for 1.1.3.4 extracted from

  • Gouda, M.D.; Singh, S.A.; Rao, A.G.; Thakur, M.S.; Karanth, N.G.
    Thermal inactivation of glucose oxidase. Mechanism and stabilization using additives (2003), J. Biol. Chem., 278, 24324-24333.
    View publication on PubMed
Search for more literature for 1.1.3.4

General Stability

General Stability Organism
K2SO4 enhances the thermal stability by primarily strengthening the hydrophobic interactions and makes the holoenzyme a more compact dimeric structure Aspergillus niger
the stabilization of the enzyme by NaCl and lysozyme is primarily the result of charge neutralization Aspergillus niger

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
160000
-
 gel filtration Aspergillus niger

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
 type VII-S
-

Subunits

Subunits Comment Organism
dimer
-
 Aspergillus niger

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 the irreversible nature of thermal inactivation is caused by a change in the state of association of apoenzyme. The dissociation of FAD results in the loss of secondary and tertiary structure, leading the unfolding and nonspecific aggregation of the enzyme molecule because of hydrophobic interactions of side chains Aspergillus niger
56
-
 half-life of native enzyme without additive: 86 min, half-life of enzyme in presence of lysozyme: 322 min, half-life of enzyme in presence of 1 M NaCl: 1806 min, half-life of enzyme in presence of 0.2 M K2SO4: 1446 min Aspergillus niger
59
-
 midpoint for thermal inactivation of residual activity and dissocation of FAD Aspergillus niger
60
-
 half-life of native enzyme without additive: 13 min, half-life of enzyme in presence of lysozyme: 46 min, half-life of enzyme in presence of 1 M NaCl: 434 min, half-life of enzyme in presence of 0.2 M K2SO4: 308 min Aspergillus niger
62
-
 midpoint for loss of secondary and tertiary structure Aspergillus niger
63
-
 half-life of native enzyme without additive: 7.5 min, half-life of enzyme in presence of lysozyme: 24 min, half-life of enzyme in presence of 1 M NaCl: 146 min, half-life of enzyme in presence of 0.2 M K2SO4: 62 min Aspergillus niger
67
-
 half-life of native enzyme without additive: 4.5 min, half-life of enzyme in presence of lysozyme: 12 min, half-life of enzyme in presence of 1 M NaCl: 58 min, half-life of enzyme in presence of 0.2 M K2SO4: 27.5 min Aspergillus niger

Cofactor

Cofactor Comment Organism Structure
FAD dissociation of FAD from the holoenzyme is responsible for the thermal inaction of the enzyme Aspergillus niger