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Literature summary extracted from

  • Soares da Silva, O.; Lira de Oliveira, R.; de Carvalho Silva, J.; Converti, A.; Souza Porto, T.
    Thermodynamic investigation of an alkaline protease from Aspergillus tamarii URM4634 a comparative approach between crude extract and purified enzyme (2018), Int. J. Biol. Macromol., 109, 1039-1044 .
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.63 additional information
-
 additional information thermodynamic and kinetic studies, simultaneous occurrence of a reversible equilibrium of enzyme unfolding, which is pushed to the right by a temperature increase, estimation of the activation energy of the hydrolysis reaction catalyzed by crude extract and purified protease as well as the respective standard enthalpy variations of reversible enzyme unfolding, overview Aspergillus tamarii

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.63 Aspergillus tamarii
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 isolated from the soil of Caatinga, in Caninde de Sao Francisco, SE, Brazil
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3.4.21.63 Aspergillus tamarii URM4634
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 isolated from the soil of Caatinga, in Caninde de Sao Francisco, SE, Brazil
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.63 native enzyme by anion exchange chromatography Aspergillus tamarii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.63 azocasein + H2O
-
 Aspergillus tamarii ?
-
 ?
3.4.21.63 azocasein + H2O
-
 Aspergillus tamarii URM4634 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.63 Alkaline protease
-
 Aspergillus tamarii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.63 28
-
 assay at Aspergillus tamarii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.21.63 50 80 when temperature is raised from 50°C to 80°C in activity assays, the specific rate constant of crude proteolytic extract thermoinactivation increases from 0.0072 to 0.0378 per min, while that of purified protease from 0.0099 to 0.0235 per min. These values, corresponding to half-life decreases from 96.3 to 18.3 min and from 70.0 to 29.5 min, respectively, allow to estimate the activation energy, enthalpy, entropy, and Gibbs free energy of thermoinactivation, overview Aspergillus tamarii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.63 7.2
-
 assay at Aspergillus tamarii