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Literature summary for 3.4.21.63 extracted from

  • Ke, Y.; Yuan, X.; Li, J.; Zhou, W.; Huang, X.; Wang, T.
    High-level expression, purification, and enzymatic characterization of a recombinant Aspergillus sojae alkaline protease in Pichia pastoris (2018), Protein Expr. Purif., 148, 24-29 .
    View publication on PubMed
Search for more literature for 3.4.21.63

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His6-tagged enzyme without signal peptide in Pichia pastoris strain KM71 Aspergillus sojae

Inhibitors

Inhibitors Comment Organism Structure
EDTA 15% inhibition at 10 mM Aspergillus sojae
Fe2+ 47% inhibition at 5 mM Aspergillus sojae
leupeptin 48% inhibition at 10 mM Aspergillus sojae
additional information no inhibition by 5 mM Mg2+ Aspergillus sojae
pepstatin 4.8% inhibition at 1 mM Aspergillus sojae
PMSF 92% inhibition at 1 mM Aspergillus sojae
SDS 60% inhibition at 0.5 mM Aspergillus sojae
Zn2+ 64% inhibition at 5 mM Aspergillus sojae

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme contains a signal peptide Aspergillus sojae
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-

Organism

Organism UniProt Comment Textmining
Aspergillus sojae A0A386IRJ1
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-
Aspergillus sojae GIM3.33 A0A386IRJ1
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Pichia pastoris strain KM71 by nickel affinity chromatography, ultrafiltration, and gel filtration Aspergillus sojae

Source Tissue

Source Tissue Comment Organism Textmining
additional information cultivation at inoculum concentration OD600 value 20.0 in 40 ml working volume (in 500 ml flasks), methanol addition (1.0% volume ratio), 0.02% biotin solution, and YNB primary concentration (13.0 g/l) results in a protease activity of 400.4 U/ml after induction for three days Aspergillus sojae
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Ala-Pro-Arg-4-nitroanilide + H2O very low activity of 3.3% compared to Ala-Ala-Pro-Phe-4-nitroanilide Aspergillus sojae Ala-Ala-Pro-Arg + 4-nitroaniline
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 ?
Ala-Ala-Pro-Arg-4-nitroanilide + H2O very low activity of 3.3% compared to Ala-Ala-Pro-Phe-4-nitroanilide Aspergillus sojae GIM3.33 Ala-Ala-Pro-Arg + 4-nitroaniline
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 ?
Ala-Ala-Pro-Asn-4-nitroanilide + H2O very low activity of 1.1% compared to Ala-Ala-Pro-Phe-4-nitroanilide Aspergillus sojae Ala-Ala-Pro-Asn + 4-nitroaniline
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 ?
Ala-Ala-Pro-Asn-4-nitroanilide + H2O very low activity of 1.1% compared to Ala-Ala-Pro-Phe-4-nitroanilide Aspergillus sojae GIM3.33 Ala-Ala-Pro-Asn + 4-nitroaniline
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 ?
Ala-Ala-Pro-Phe-4-nitroanilide + H2O
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 Aspergillus sojae Ala-Ala-Pro-Phe + 4-nitroaniline
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 ?
Ala-Ala-Pro-Phe-4-nitroanilide + H2O
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 Aspergillus sojae GIM3.33 Ala-Ala-Pro-Phe + 4-nitroaniline
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 ?
Bovine serum albumin + H2O
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 Aspergillus sojae ?
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 ?
Bovine serum albumin + H2O
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 Aspergillus sojae GIM3.33 ?
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 ?
additional information the recombinan enzyme shows a broad substrate specificity for natural proteins (e.g. soy proteins) and synthetic peptide substrates, and prefers substrates at P1 position with large hydrophobic side-chain groups. Ala-Ala-Pro-Glu-4-nitroanilide and glutin are a poor substrate Aspergillus sojae ?
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 ?
additional information the recombinan enzyme shows a broad substrate specificity for natural proteins (e.g. soy proteins) and synthetic peptide substrates, and prefers substrates at P1 position with large hydrophobic side-chain groups. Ala-Ala-Pro-Glu-4-nitroanilide and glutin are a poor substrate Aspergillus sojae GIM3.33 ?
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 ?

Subunits

Subunits Comment Organism
? x * 41318, recombinant His6-tagged enzyme without signal peptide, sequence calculation, x * 35200, recombinant His6-tagged enzyme without signal peptide, SDS-PAGE Aspergillus sojae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
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-
 Aspergillus sojae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
 purified recombinant enzyme, 60 min, over 50% activity remaining Aspergillus sojae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
-
 Aspergillus sojae

pH Stability

pH Stability pH Stability Maximum Comment Organism
7 10 purified recombinant enzyme, stable at Aspergillus sojae

General Information

General Information Comment Organism
additional information compared to papain (8.7%) and alcalase (12.2%), the degree of hydrolysis of rAp to soy protein isolate is 16.5% Aspergillus sojae