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Literature summary extracted from

  • Gao, X.; Yin, Y.; Yan, J.; Zhang, J.; Ma, H.; Zhou, C.
    Separation, biochemical characterization and salt-tolerant mechanisms of alkaline protease from Aspergillus oryzae (2019), J. Sci. Food. Agric., 99, 3359-3366 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.4.21.63 food industry the salt tolerance of proteases secreted by Aspergillus oryzae 3.042 closely relates to the utilization of raw materials and the quality of soy sauce Aspergillus oryzae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.63 Ag+ 72% inhibition at 1 mM Aspergillus oryzae
3.4.21.63 Cu2+ 7% inhibition at 1 mM Aspergillus oryzae
3.4.21.63 Hg2+ 73% inhibition at 1 mM Aspergillus oryzae
3.4.21.63 Mn2+ 15% inhibition at 1 mM Aspergillus oryzae
3.4.21.63 additional information no or poor effect by 5 mM of EDTA, o-phenanthroline, bestatin, or 1 mM Zn2+ Aspergillus oryzae
3.4.21.63 TLCK 57% inhibition at 5 mM Aspergillus oryzae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.63 additional information
-
additional information Michaelis-Menten kinetics, overview Aspergillus oryzae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.63 Ca2+ activates 26% at 1 mM Aspergillus oryzae
3.4.21.63 Mg2+ activates 17% at 1 mM Aspergillus oryzae
3.4.21.63 additional information a metal-ion-independent serine protease Aspergillus oryzae
3.4.21.63 NaCl over 20% relative activity of the enzyme remains in the presence of 3.0 mo/l NaCl after 7 days, but its Km and Vmax are only mildly influenced. The salt-tolerant mechanisms of the enzyme might be due to more salt bridges, higher proportion of ordered secondary structures and stronger hydrophobic amino acid residues in the interior Aspergillus oryzae

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.63 Aspergillus oryzae
-
-
-
3.4.21.63 Aspergillus oryzae 3.042
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.21.63 native salt-tolerant alkaline protease 28fold from Aspergllus oryzae strain 3.042 by ammonium sulfate fractionation, cation exchange chromatography, and gel filtration Aspergillus oryzae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.21.63 632.6
-
purified native enzyme, pH 9.0, 28°C Aspergillus oryzae

Subunits

EC Number Subunits Comment Organism
3.4.21.63 ? x * 28980, mass spectromtery Aspergillus oryzae
3.4.21.63 More enzyme structure homology modeling Aspergillus oryzae

Synonyms

EC Number Synonyms Comment Organism
3.4.21.63 Alkaline protease
-
Aspergillus oryzae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.63 40
-
-
Aspergillus oryzae

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.21.63 20 70 activity range, profile overview Aspergillus oryzae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.21.63 45
-
purified enzyme, completely stable up to Aspergillus oryzae
3.4.21.63 55
-
purified enzyme, loss of 30% activity Aspergillus oryzae
3.4.21.63 65
-
purified enzyme, loss of 60% activity Aspergillus oryzae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.63 9
-
-
Aspergillus oryzae

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.21.63 7 12 over 50% of maximal activity within this range, profile overview Aspergillus oryzae

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.4.21.63 7 11 purified enzyme, over 60% activity remaining, maximally stable at pH 9.0, profile overview Aspergillus oryzae

General Information

EC Number General Information Comment Organism
3.4.21.63 additional information enzyme structure homology modeling. The active center of the alkaline protease is established by three amino acid residues Asp41, His72, and Ser228, based on the result of protein sequence alignment between the alkaline protease and cuticle-degrading protease from north american fungi, three-dimensional structures, overview Aspergillus oryzae