Literature summary for 3.4.21.63 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 .

Search for more literature for 3.4.21.63

Application

Application	Comment	Organism
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

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

KM Value [mM]

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	activates 26% at 1 mM	Aspergillus oryzae
Mg2+	activates 17% at 1 mM	Aspergillus oryzae
additional information	a metal-ion-independent serine protease	Aspergillus oryzae
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

Organism	UniProt	Comment	Textmining
Aspergillus oryzae	-	-	-
Aspergillus oryzae 3.042	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
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]

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

Subunits

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

Synonyms

Synonyms	Comment	Organism
Alkaline protease	-	Aspergillus oryzae

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

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

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
9	-	-	Aspergillus oryzae

pH Range

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

pH Stability

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

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)