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3-phenyllactic acid + H2O
?
-
methyl esters and its ring-substituted derivative hydrolyzed with excellent enantioselectivities
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
Acetyl-Ala methyl ester + H2O
Acetyl-Ala + methanol
Acetyl-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala + methanol
Acetyl-Ala-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala-Ala + methanol
Acetyl-Ala-Ala-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala-Ala-Ala + methanol
Acetyl-Ala-Ala-Phe methyl ester + H2O
Acetyl-Ala-Ala-Phe + methanol
Acetyl-Ala-Phe methyl ester + H2O
Acetyl-Ala-Phe + methanol
acetyl-L-tyrosine ethyl ester + H2O
acetyl-L-tyrosine + ethanol
-
-
-
-
?
Acetyl-Phe methyl ester + H2O
Acetyl-Phe + methanol
Ala-Ala-Pro-Arg-4-nitroanilide + H2O
Ala-Ala-Pro-Arg + 4-nitroaniline
Ala-Ala-Pro-Asn-4-nitroanilide + H2O
Ala-Ala-Pro-Asn + 4-nitroaniline
Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Ala-Ala-Pro-Phe + 4-nitroaniline
Benzoylarginine ethyl ester + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Ala-Ala-Lys methyl ester + H2O
Benzyloxycarbonyl-Ala-Ala-Lys + methanol
Benzyloxycarbonyl-Ala-Lys methyl ester + H2O
Benzyloxycarbonyl-Ala-Lys + methanol
Benzyloxycarbonyl-Gly-Lys methyl ester + H2O
Benzyloxycarbonyl-Gly-Lys + methanol
Benzyloxycarbonyl-Leu-Lys methyl ester + H2O
Benzyloxycarbonyl-Leu-Lys + methanol
Benzyloxycarbonyl-Lys methyl ester + H2O
Benzyloxycarbonyl-Lys + methanol
Benzyloxycarbonyl-Phe-Lys methyl ester + H2O
Benzyloxycarbonyl-Phe-Lys + methanol
Bovine serum albumin + H2O
?
bovine serum fibrin + H2O
?
-
-
-
?
Carbobenzoxy-Leu-Gly-NH2 + H2O
Carbobenzoxy-Leu-Gly + NH3
-
-
-
?
Carbobenzoxy-Pro-Leu-NH2 + H2O
Carbobenzoxy-Pro-Leu + NH3
-
-
-
?
casein + H2O
hydrolyzed casein
defatted soybean complex medium + H2O
?
Egg albumin + H2O
Hydrolyzed egg albumin
-
-
-
-
?
Fibrin + H2O
Hydrolyzed fibrin
-
-
-
-
?
Fibrinogen + H2O
Hydrolyzed fibrinogen
-
-
-
-
?
Gelatin + H2O
Hydrolyzed gelatin
Hemoglobin + H2O
Hydrolyzed hemoglobin
Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH2 + H2O
Ile-Gln-Asn-Cys-Pro-Leu + Gly-NH2
-
-
-
?
L-Leu 4-nitroanilide hydrochloride + H2O
?
-
-
-
-
?
mandelic acid + H2O
?
-
only low enantioselectivities
-
-
?
N-Acetyl amino acid ester + H2O
?
-
hydrolysis decreases in the order of Phe/ Tyr, Trp, Met, Leu, Lys, His, Val/ Gly
-
-
?
N-Acetyl-L-tyrosine ethyl ester + H2O
?
N-acetyl-L-tyrosine ethylester + H2O
?
N-Benzoyl-L-arginine ethyl ester + H2O
?
-
-
-
-
?
N-Cbz-L-Asp + sec-butanol
N-Cbz-L-Asp-sec-butyl ester
-
-
-
r
N-Cbz-L-Tyr + 1-phenylethanol
N-Cbz-L-Tyr-1-phenylethyl ester
-
-
-
?
N-Cbz-L-Tyr + sec-butanol
N-Cbz-L-Tyr-sec-butyl ester
-
-
-
r
Oxidized insulin A-chain + H2O
Hydrolyzed oxidized insulin A-chain
-
at 0øC the enzyme cleaves only the bond Glu17-Asn18
-
-
?
Oxidized insulin B-chain + H2O
?
-
eight cleavage sites of the enzyme in oxidized insulin B-chain are determined by mass spectrometry, and five of them have high hydrophobic amino acid affinity
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
Poly-L,alpha-glutamic acid + H2O
?
-
-
-
-
?
Poly-L-lysine + H2O
?
-
-
-
-
?
Protamine + H2O
Hydrolyzed protamine
-
-
-
-
?
Serum albumin + H2O
Hydrolyzed serum albumin
-
-
-
-
?
Soybean 11S globulin + H2O
Hydrolyzed soybean 11S globulin
-
-
-
-
?
Soybean protein + H2O
Hydrolyzed soybean protein
-
-
-
-
?
additional information
?
-
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
Acetyl-Ala methyl ester + H2O
Acetyl-Ala + methanol
-
-
-
-
?
Acetyl-Ala methyl ester + H2O
Acetyl-Ala + methanol
-
-
-
-
?
Acetyl-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala + methanol
-
-
-
?
Acetyl-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala + methanol
-
-
-
?
Acetyl-Ala-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala-Ala + methanol
-
-
-
-
?
Acetyl-Ala-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala-Ala + methanol
-
-
-
-
?
Acetyl-Ala-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala-Ala + methanol
-
-
-
-
?
Acetyl-Ala-Ala-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala-Ala-Ala + methanol
-
-
-
-
?
Acetyl-Ala-Ala-Ala-Ala methyl ester + H2O
Acetyl-Ala-Ala-Ala-Ala + methanol
-
-
-
-
?
Acetyl-Ala-Ala-Phe methyl ester + H2O
Acetyl-Ala-Ala-Phe + methanol
-
-
-
-
?
Acetyl-Ala-Ala-Phe methyl ester + H2O
Acetyl-Ala-Ala-Phe + methanol
-
-
-
-
?
Acetyl-Ala-Phe methyl ester + H2O
Acetyl-Ala-Phe + methanol
-
-
-
?
Acetyl-Ala-Phe methyl ester + H2O
Acetyl-Ala-Phe + methanol
-
-
-
?
Acetyl-Phe methyl ester + H2O
Acetyl-Phe + methanol
-
-
-
-
?
Acetyl-Phe methyl ester + H2O
Acetyl-Phe + methanol
-
-
-
-
?
Ala-Ala-Pro-Arg-4-nitroanilide + H2O
Ala-Ala-Pro-Arg + 4-nitroaniline
very low activity of 3.3% compared to Ala-Ala-Pro-Phe-4-nitroanilide
-
-
?
Ala-Ala-Pro-Arg-4-nitroanilide + H2O
Ala-Ala-Pro-Arg + 4-nitroaniline
very low activity of 3.3% compared to Ala-Ala-Pro-Phe-4-nitroanilide
-
-
?
Ala-Ala-Pro-Asn-4-nitroanilide + H2O
Ala-Ala-Pro-Asn + 4-nitroaniline
very low activity of 1.1% compared to Ala-Ala-Pro-Phe-4-nitroanilide
-
-
?
Ala-Ala-Pro-Asn-4-nitroanilide + H2O
Ala-Ala-Pro-Asn + 4-nitroaniline
very low activity of 1.1% compared to Ala-Ala-Pro-Phe-4-nitroanilide
-
-
?
Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
Ala-Ala-Pro-Phe-4-nitroanilide + H2O
Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
97% activity compared to casein
-
-
?
azocasein + H2O
?
-
97% activity compared to casein
-
-
?
Benzyloxycarbonyl-Ala-Ala-Lys methyl ester + H2O
Benzyloxycarbonyl-Ala-Ala-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Ala-Ala-Lys methyl ester + H2O
Benzyloxycarbonyl-Ala-Ala-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Ala-Lys methyl ester + H2O
Benzyloxycarbonyl-Ala-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Ala-Lys methyl ester + H2O
Benzyloxycarbonyl-Ala-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Gly-Lys methyl ester + H2O
Benzyloxycarbonyl-Gly-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Gly-Lys methyl ester + H2O
Benzyloxycarbonyl-Gly-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Leu-Lys methyl ester + H2O
Benzyloxycarbonyl-Leu-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Leu-Lys methyl ester + H2O
Benzyloxycarbonyl-Leu-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Lys methyl ester + H2O
Benzyloxycarbonyl-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Lys methyl ester + H2O
Benzyloxycarbonyl-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Phe-Lys methyl ester + H2O
Benzyloxycarbonyl-Phe-Lys + methanol
-
-
-
-
?
Benzyloxycarbonyl-Phe-Lys methyl ester + H2O
Benzyloxycarbonyl-Phe-Lys + methanol
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
18% activity compared to casein
-
-
?
Bovine serum albumin + H2O
?
-
18% activity compared to casein
-
-
?
Bovine serum albumin + H2O
?
-
-
-
?
casein + H2O
?
-
-
-
?
casein + H2O
?
-
artificial substrate
-
-
?
casein + H2O
?
-
artificial substrate
-
-
?
casein + H2O
?
-
best substrate
-
-
?
casein + H2O
?
-
best substrate
-
-
?
casein + H2O
?
-
best substrate
-
-
?
casein + H2O
?
-
best substrate
-
-
?
casein + H2O
?
-
the enzyme has a high affinity for the casein, best substrate
-
-
?
casein + H2O
?
-
the enzyme has a high affinity for the casein, best substrate
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
?
casein + H2O
hydrolyzed casein
-
active centre of the enzyme contains serine residues
-
-
?
casein + H2O
hydrolyzed casein
-
active centre of the enzyme contains serine residues
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
-
?
Collagen + H2O
?
-
-
-
?
defatted soybean complex medium + H2O
?
-
increase in production by adding lactose, casitone or casein, even glucose, starch, sucrose, maltose, or arabinose
-
?
defatted soybean complex medium + H2O
?
-
increase in production by adding lactose, casitone or casein, even glucose, starch, sucrose, maltose, or arabinose
-
?
Gelatin + H2O
?
-
low activity
-
-
?
Gelatin + H2O
?
-
low activity
-
-
?
Gelatin + H2O
?
-
the active enzyme degrades the copolymerized gelatin with high activity
-
-
?
Gelatin + H2O
?
-
the active enzyme degrades the copolymerized gelatin with high activity
-
-
?
Gelatin + H2O
?
-
28% activity compared to casein
-
-
?
Gelatin + H2O
?
-
28% activity compared to casein
-
-
?
Gelatin + H2O
Hydrolyzed gelatin
-
-
-
-
?
Gelatin + H2O
Hydrolyzed gelatin
-
-
-
-
?
Gelatin + H2O
Hydrolyzed gelatin
-
-
-
-
?
Hemoglobin + H2O
?
-
60% activity compared to casein
-
-
?
Hemoglobin + H2O
?
-
60% activity compared to casein
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
-
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
-
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
-
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
-
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
-
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
alpha-chain
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
alpha-chain
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
-
-
-
?
hen egg albumin + H2O
?
-
-
-
-
?
hen egg albumin + H2O
?
-
-
-
-
?
N-Acetyl-L-tyrosine ethyl ester + H2O
?
-
-
-
-
?
N-Acetyl-L-tyrosine ethyl ester + H2O
?
-
-
-
-
?
N-acetyl-L-tyrosine ethylester + H2O
?
-
low activity
-
-
?
N-acetyl-L-tyrosine ethylester + H2O
?
-
low activity
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
at 0øC the enzyme cleaves only the bond Leu15-Tyr16
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
-
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
-
-
-
?
additional information
?
-
-
no exoprotease activity
-
-
?
additional information
?
-
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
additional information
?
-
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
additional information
?
-
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
additional information
?
-
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
additional information
?
-
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
additional information
?
-
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
additional information
?
-
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
additional information
?
-
-
secreted Aspergillus fumigatus protease Alp1 degrades human complement proteins in culture supernatant C3, C4, C5, and C1q as well as immunoglobulin G. C4 is completely degraded. Degradation of C5 and C1q is also observed but is less prominent
-
-
?
additional information
?
-
-
secreted Aspergillus fumigatus protease Alp1 degrades human complement proteins in culture supernatant C3, C4, C5, and C1q as well as immunoglobulin G. C4 is completely degraded. Degradation of C5 and C1q is also observed but is less prominent
-
-
?
additional information
?
-
-
the esterase activity is markedly promoted by elongating the peptide chain from P1 to P2 or P3 with alanine, irrespectively of the kind of the amino acid residue at the P1-position
-
-
?
additional information
?
-
-
leucine or phenylalanine is most efficient at the P2-position
-
-
?
additional information
?
-
-
solid cereal substrates
-
-
?
additional information
?
-
-
action of Aspergillus oryzae protease on whey proteins, analysis of the enzymatic hydrolysates, method evaluation and peptide profile determined by size exclusion HPLC, overview. The enzyme shows a strong negative correlation between the large peptide content and the degree of hydrolysis
-
-
?
additional information
?
-
-
the enzyme shows a high degree of hydrolysis with soybean protein (8.8%) and peanut protein (11.1%) compared to papain and alcalase
-
-
?
additional information
?
-
-
solid cereal substrates
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
the esterase activity is markedly promoted by elongating the peptide chain from P1 to P2 or P3 with alanine, irrespectively of the kind of the amino acid residue at the P1-position
-
-
?
additional information
?
-
-
in the hydrolysis of natural proteins, the enzyme liberates relatively large peptides and traces (endo-type)
-
-
?
additional information
?
-
-
leucine or phenylalanine is most efficient at the P2-position
-
-
?
additional information
?
-
-
relatively high specificity for lysine, tyrosine, histidine, arginine and phenylalanine residues
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
-
specificity overview
-
-
?
additional information
?
-
the enzyme performs well in removing an egg protein stain when supplemented into a commercial powder detergent
-
-
?
additional information
?
-
activity with gelatin
-
-
?
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2-propanol
-
inhibits at 30% v/v
4-nitrophenyl acetate
-
increasing concentrations of the ester inhibit casein hydrolysis
acetonitrile
48% inhibition at 10%
Ba2+
-
some inhibition at 10 mM
benzamidine
slightly inhibits recombinant and native enzyme
Benzyloxycarbonyl-Ala-Gly-PheCH2Cl
Ca2+
-
some inhibition at 10 mM
Cd2+
-
some inhibition at 1 mM
cetyltrimethyl ammonium bromide
-
-
chloroform
-
loss of 45-88.5% activity at 15-50% v/v after 24 h, loss of 31-21% activity after 1 h
DTNB
-
52-57% inhibition at 1-5 mM
formaldehyde
-
loss of 27-13% activity at 15-50% v/v after 24 h, loss of 46-47% activity after 1 h
iodoacetamide
-
5.2% inhibition at 5 mM
iodoacetic acid
-
strong inhibition at 5 mM
n-butanol
-
inhibition of esterolytic activity
N-diazoacetylnorleucine methyl ester
-
8.3% inhibition at 5 mM
N-ethylmaleimide
-
11.2% inhibition at 5 mM
n-Propanol
-
inhibition of esterolytic activity
N-tosyl-L-lysine chloromethyl ketone
inhibitor of recombinant and native enzyme
Na+
-
7.5% inhibition at 5 mM
Pb2+
-
some inhibition at 10 mM
pepstatin
4.8% inhibition at 1 mM
Phenylmethyl sulfonylfluoride
-
complete inhibition
phenylmethylsulfonyl fluoride
Sodium azide
-
22.0% inhibition at 5 mM
sodium lauryl sulfate
-
-
Sr2+
-
some inhibition at 10 mM
tosyl-L-lysylchloromethyl ketone
-
6.7% inhibition at 5 mM
TPCK
-
moderately inhibits
Trypsin inhibitor
-
moderately inhibits
-
Tween 80
-
72% inhibition at 1-5 mM
acetone
-
loss of 64-74% activity at 15-50% v/v after 24 h, loss of 27-70% activity after 1 h
acetone
13% inhibition at 10%
Ag+
-
-
Ag+
strong inhibitor of recombinant and native enzyme
Ag+
-
72% inhibition at 1 mM
Ag+
-
about 19% inhibition at 1-10 mM
Benzyloxycarbonyl-Ala-Gly-PheCH2Cl
-
-
Benzyloxycarbonyl-Ala-Gly-PheCH2Cl
-
-
butanol
-
50% inhibition after 2 h
butanol
-
loss of 40-68% activity at 15-50% v/v after 24 h, loss of 40-47% activity after 1 h
Co2+
-
some inhibition at 1 mM
Co2+
-
about 10% inhibition at 5 mM
Co2+
-
8% inhibition at 10 mM
CTAB
70% inhibition at 1.0%
CTAB
50% inhibition at 1.0%
Cu2+
-
some inhibition at 1 mM
Cu2+
-
over 90% inhibition at 5 mM
Cu2+
inhibitor of recombinant and native enzyme
Cu2+
-
7% inhibition at 1 mM
DFP
-
-
DMSO
-
inhibits at 30% v/v
DMSO
-
loss of 41-53% activity at 15-50% v/v after 24 h, loss of 21-48% activity after 1 h
DTT
-
9.9% inhibition at 5 mM
EDTA
-
-
EDTA
slightly inhibits recombinant and native enzyme
EDTA
15% inhibition at 10 mM
EDTA
-
complete inhibition
EDTA
-
12.7% inhibition at 5 mM
EDTA
-
complete inhibition at 5 mM, 50% at 1 mM
ethanol
-
reversible inhibition
ethanol
-
loss of 55-78% activity at 15-50% v/v after 24 h, loss of 8-55% activity after 1 h
ethanol
39.5% inhibition at 10%
Fe2+
-
-
Fe2+
47% inhibition at 5 mM
Fe2+
-
45% inhibition at 10 mM, 33.5% at 5 mM
Fe3+
-
-
Fe3+
-
18.9% inhibition at 5 mM
H2O2
-
-
H2O2
-
73-74% inhibition at 1-5 mM
Hg2+
-
some inhibition at 1 mM
Hg2+
-
complete inhibition at 5 mM
Hg2+
strong inhibitor of recombinant and native enzyme
Hg2+
-
73% inhibition at 1 mM
Hg2+
-
25.2% inhibition at 5 mM
Isopropanol
-
inhibits at 30% v/v
Isopropanol
-
loss of 39-45% activity at 15-50% v/v after 24 h, loss of about 50% activity after 1 h
Isopropanol
68% inhibition at 10%
leupeptin
-
68% inhibition of AP30 at 0.05 mM
leupeptin
48% inhibition at 10 mM
methanol
-
inhibition of esterolytic activity
methanol
-
loss of 75-100% activity at 15-50% v/v after 24 h, loss of 44-93% activity after 1 h
Mn2+
-
about 30% inhibition at 5 mM
Mn2+
inhibitor of recombinant and native enzyme
Mn2+
-
15% inhibition at 1 mM
Mn2+
-
14.1% inhibition at 5 mM
N-bromosuccinimide
-
-
N-bromosuccinimide
-
50.3% inhibition at 5 mM
Ni2+
-
some inhibition at 1 mM
Ni2+
-
about 20% inhibition at 5 mM
Ni2+
-
32% inhibition at 10 mM, 28% at 5 mM
phenylmethylsulfonyl fluoride
-
100% inhibition of AP30 at 5 mM
phenylmethylsulfonyl fluoride
-
completely inhibits
phenylmethylsulfonyl fluoride
strong inhibitor of recombinant and native enzyme
PMSF
-
-
PMSF
-
strong inhibition at 5 mM
PMSF
92% inhibition at 1 mM
PMSF
-
83.7% inhibition at 5 mM
PMSF
-
complete inhibition at 5 mM, 97% at 1 mM
Potato inhibitor
-
-
-
SDS
complete inhibition at 1.0%
SDS
-
strong inhibition at 0.5%
SDS
60% inhibition at 0.5 mM
SDS
-
complete inhibition at 5 mM, 96% at 1 mM
SDS
70% inhibition at 1.0%
TLCK
-
moderately inhibits
TLCK
-
57% inhibition at 5 mM
Triton X-100
10% inhibition at 1.0%
Triton X-100
-
45% inhibition at 5 mM, 39% at 1 mM
Tween 20
5% inhibition at 1.0%
Tween 20
-
66% inhibition at 5 mM, 39% at 1 mM
Urea
-
slight inhibition at 5 mM
Urea
-
4.5% inhibition at 5 mM
Urea
-
71% inhibition at 1 mM, 95.5% at 8 mM
Zn2+
-
some inhibition at 10 mM
Zn2+
-
about 20% inhibition at 5 mM
Zn2+
inhibitor of recombinant and native enzyme
Zn2+
64% inhibition at 5 mM
Zn2+
-
10.9% inhibition at 5 mM
Zn2+
-
40% inhibition at 10 mM, 38% at 1-5 mM
additional information
-
metal chelating agents; monoiodoacetic acid; not: sulfhydryl reagents; PCMB
-
additional information
-
cysteine; EDTA; KCN; not: sulfhydryl reagents; PCMB
-
additional information
-
poor inhibition by Ca2+ at 5 mM
-
additional information
-
the enzyme is completely stable in presence of laundry detergents, overview
-
additional information
-
cysteine; EDTA; KCN; not: sulfhydryl reagents; PCMB
-
additional information
-
EDTA
-
additional information
-
not inhibited by Cu2+, Sn2+, Ba2+, Co2+, Li+, benzamidine, beta-ME, cysteine, EDTA and 1,10-phenathroline
-
additional information
-
Triton X-100 and PMSF have no inhibitory effect on the enzyme activity
-
additional information
-
no or poor effect by 5 mM of EDTA, o-phenanthroline, bestatin, or 1 mM Zn2+
-
additional information
no inhibition by 5 mM Mg2+
-
additional information
-
not inhibitory: commercial detergents such as Vim and Avis
-
additional information
-
cysteine; EDTA; KCN; not: sulfhydryl reagents; PCMB
-
additional information
-
no effect by H2O2 and NaClO
-
additional information
no inhibition by Tween 20 and Triton X-100 at 1.0%
-
additional information
no or poor inhibition by Ba2+, Cr3+, K+, Fe3+, Ca2+, Zn2+, and Mg2+, all at 1 mM. No inhibition by methanol at 10%
-
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0 - 40
purified recombinant enzyme, 2.5 h, completely stable at
20 - 80
-
purified native extracellular enzyme, over 50% activity remaining after 15-30 min. After 60-min incubation, the enzyme preserves 70.74%, 54.22%, 94.82%, and 98.47% of its activity at 40°C, 50°C, 60°C, and 70°C, respectively
30 - 40
-
partially purified enzyme, stable at, retention of 96% activity after 1 h of incubation at 40°C
35
-
pH 7.5, highest stability
40 - 50
-
purified enzyme, 24 h, completely stable at
50 - 55
-
activity is reduced by 15% at 50°C and by 66% at 55°C
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
60 - 70
-
purified native extracellular enzyme, 1 h, 90% activity remaining
60 - 90
-
purified secreted enzyme, 1 h, completely stable at
65
-
purified enzyme, loss of 60% activity
70
purified recombinant enzyme, 30 min, inactivation
40
-
half-life 90 min
40
purified recombinant enzyme, 60 min, over 50% activity remaining
40
purified enzyme, 70% activity remaining after 60 min, over 80% activity after 5-30 min
45
-
moderate inactivation up to
45
-
84% residual activity after 1 h of incubation at 45°C
45
-
purified enzyme, completely stable up to
50
-
half-life 18 min
50
purified enzyme, over 80% activity remaining after 60 min
50
-
purified recombinant truncated neutral protease I, 120 min, over 90% activity remaining
50
-
purified enzyme, half-life is 100 min
50
purified enzyme, loss of 95% activity after 60 min, loss of 75% after 30 min, and 50% after 15 min
50
purified recombinant enzyme, 30 min, 55% activity remaining, inactivation after 2.5 h
55
-
10 min, most stable at pH 6.0
55
purified enzyme, 60 min, loss of 65% activity, 65% activity remaining after 30 min
55
-
53% residual activity after 1 h of incubation at 55°C
55
-
immobilized enzyme retains 86% of its activity while the free enzyme retains only 10%
55
-
purified enzyme, loss of 30% activity
55
-
pH 7.5, 10 min, complete inactivation after incubation in 0.01 M sodium phosphate, Aspergillus sydowi
55
purified enzyme, 15 min, inactivation, 90% activity remaining after 5 min
60
purified enzyme, 18 min, inactivation
60
purified enzyme, 5 min, inactivation
60
purified recombinant enzyme, 30 min, 40% activity remaining, inactivation after 2 h
additional information
-
2 mM Ca2+ protect against heat denaturation
additional information
-
thermal stability profile, overview
additional information
-
the thermal stability of the enzyme is substantially improved by NaCl
additional information
the native enzyme exhibits a better thermostability than the recombinant enzyme
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detergent
-
enzyme is highly compatible with commercial detergents such as Vim and Avis and may find application in laundry detergents
detergent
-
alkaline proteases are primarily used in the detergent industry. The addition of the protease to the detergent Super wheel improved its blood stain removal
detergent
peptidases are important additives in detergent formulation to remove protein stains such as those from blood, egg, and food debris
detergent
peptidases are important additives in detergent formulation to remove protein stains such as those from blood, egg, and food debris
detergent
-
peptidases are important additives in detergent formulation to remove protein stains such as those from blood, egg, and food debris
-
detergent
-
peptidases are important additives in detergent formulation to remove protein stains such as those from blood, egg, and food debris
-
detergent
-
alkaline proteases are primarily used in the detergent industry. The addition of the protease to the detergent Super wheel improved its blood stain removal
-
detergent
-
peptidases are important additives in detergent formulation to remove protein stains such as those from blood, egg, and food debris
-
detergent
-
peptidases are important additives in detergent formulation to remove protein stains such as those from blood, egg, and food debris
-
detergent
-
peptidases are important additives in detergent formulation to remove protein stains such as those from blood, egg, and food debris
-
detergent
-
peptidases are important additives in detergent formulation to remove protein stains such as those from blood, egg, and food debris
-
food industry
-
the enzyme is efficient in producing antihypertensive peptide IPP from beta-casein and a potential debittering agent. The high degree of hydrolysis of the enzyme to soybean protein (8.8%) and peanut protein (11.1%) compared to papain and alcalase makes it a good candidate in the processing of oil industry byproducts
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
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
-
industry
-
immobilization of the enzyme as an important biotechnological aspect
industry
-
optimization of protease production in fermentation medium with optimal salt, nitrogen and carbon concentrations
industry
-
possible use of the enzyme in detergent industry and peptide synthesis due to its compatibility with several detergents, oxidants and organic solvents
industry
alkaline proteases are a major group of industrial enzymes that hydrolyze proteins into short peptides and amino acids, and catalyze peptide synthesis
industry
peptidases are important enzymes with applications in many industrial sectors, such as the production of cheese, meat, fish, and wine, protein hydrolysates, the pharmaceutical industry, the leather industry, cosmetics, and fine chemicals
industry
peptidases are important enzymes with applications in many industrial sectors, such as the production of cheese, meat, fish, and wine, protein hydrolysates, the pharmaceutical industry, the leather industry, cosmetics, and fine chemicals
industry
-
peptidases are important enzymes with applications in many industrial sectors, such as the production of cheese, meat, fish, and wine, protein hydrolysates, the pharmaceutical industry, the leather industry, cosmetics, and fine chemicals
-
industry
-
optimization of protease production in fermentation medium with optimal salt, nitrogen and carbon concentrations
-
industry
-
peptidases are important enzymes with applications in many industrial sectors, such as the production of cheese, meat, fish, and wine, protein hydrolysates, the pharmaceutical industry, the leather industry, cosmetics, and fine chemicals
-
industry
-
peptidases are important enzymes with applications in many industrial sectors, such as the production of cheese, meat, fish, and wine, protein hydrolysates, the pharmaceutical industry, the leather industry, cosmetics, and fine chemicals
-
industry
-
peptidases are important enzymes with applications in many industrial sectors, such as the production of cheese, meat, fish, and wine, protein hydrolysates, the pharmaceutical industry, the leather industry, cosmetics, and fine chemicals
-
industry
-
peptidases are important enzymes with applications in many industrial sectors, such as the production of cheese, meat, fish, and wine, protein hydrolysates, the pharmaceutical industry, the leather industry, cosmetics, and fine chemicals
-
industry
-
peptidases are important enzymes with applications in many industrial sectors, such as the production of cheese, meat, fish, and wine, protein hydrolysates, the pharmaceutical industry, the leather industry, cosmetics, and fine chemicals
-
industry
-
immobilization of the enzyme as an important biotechnological aspect
-
industry
-
possible use of the enzyme in detergent industry and peptide synthesis due to its compatibility with several detergents, oxidants and organic solvents
-
nutrition
-
used in food processing, strain U1521 assumes industrial and economic importance
nutrition
-
used in food processing, strain U1521 assumes industrial and economic importance
-
additional information
-
the produced enzyme is able to recover silver from used X-ray film under optimized condition, overview
additional information
-
the produced enzyme is able to recover silver from used X-ray film under optimized condition, overview
-
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Turkova, J.; Mikes, O.; Hayashi, K.; Danno, G.; Polgar, L.
Alkaline proteinases of the genus Aspergillus
Biochim. Biophys. Acta
257
257-263
1972
Aspergillus oryzae, Aspergillus sojae, Aspergillus sulphureus
brenda
Spadari, S.; Subramanian, A.R.; Kalnitsky, G.
Highly restricted specificity of the serine proteinase aspergillopeptidase B
Biochim. Biophys. Acta
359
267-272
1974
Aspergillus oryzae
brenda
Morihara, K.; Oka, T.; Tsuzuki, H.
Comparative study of various serine alkaline proteinases from microorganisms. Esterase activity against N-acylated peptide ester substrates
Arch. Biochem. Biophys.
165
72-79
1974
Aspergillus melleus, Aspergillus sojae
brenda
Nakagawa, Y.
Alkaline proteinases from Aspergillus
Methods Enzymol.
19
581-591
1970
Aspergillus flavus, Aspergillus oryzae, Aspergillus sojae, Aspergillus sydowii
-
brenda
Hayashi, K.; Terada, M.
Some characteristics of hydrolysis of synthetic substrates and proteins by the alkaline proteases from Aspergillus sojae
Agric. Biol. Chem.
36
1755-1765
1972
Aspergillus sojae
-
brenda
Nasuno, S.; Ohara, T.
Purification of alkaline proteinase from Aspergillus candidus
Agric. Biol. Chem.
36
1791-1796
1972
Aspergillus candidus
-
brenda
Ohara, T.; Nasuno, S.
Enzymic properties of alkaline proteinase from Aspergillus candidus
Agric. Biol. Chem.
36
1797-1802
1972
Aspergillus candidus
-
brenda
Impoolsup, A.; Bhumiratana, A.; Flegel, T.W.
Isolation of alkaline and neutral proteases from Aspergillus flavus var. columnaris, a soy sauce koji mold
Appl. Environ. Microbiol.
42
619-628
1981
Aspergillus flavus
brenda
Nakadai, T.; Nasuno, S.; Iguchi, N.
Purification and properties of alkaline proteinase from Aspergillus oryzae
Agric. Biol. Chem.
37
2685-2694
1973
Aspergillus oryzae
-
brenda
Danno, G.; Natake, M.
Substrate specificity of alkaline proteinases from Aspergillus sydowi and Aspergillus sulphureus
Agric. Biol. Chem.
37
1493-1496
1973
Aspergillus sulphureus, Aspergillus sydowii
-
brenda
Kundu, A.K.; Manna, S.
Purification and characterization of extracellular proteinases of Aspergillus oryzae
Appl. Microbiol.
30
507-513
1975
Aspergillus oryzae, Aspergillus oryzae EI212
brenda
Nakatani, H.; Fujiwake, H.; Hiromi, K.
Interaction of Asp. melleus Semi-alkaline protease with benzeneboronic acid
J. Biochem.
81
1269-1272
1977
Aspergillus melleus
brenda
Ogundero, V.W.; Osunlaja, S.O.
The purification and activities of an alkaline protease of Aspergillus clavatus from Nigerian poultry feeds
J. Basic Microbiol.
26
241-248
1986
Aspergillus clavatus
brenda
Feinstein, G.; Gertler, A.
Isolation of alkaline proteinases from Aspergillus oryzae by one-step affinity chromatography on ovoinhibitor-sepharose column
Biochim. Biophys. Acta
309
196-202
1973
Aspergillus oryzae
brenda
Klapper, B.F.; Jameson, D.M.; Mayer, R.M.
The purification and properties of an extracellular protease from Aspergillus oryzae NRRL 2160
Biochim. Biophys. Acta
304
505-512
1973
Aspergillus oryzae, Aspergillus oryzae NRRL 2160
brenda
Ku, H.C.; Wyborny, L.; Kalnitsky, G.
Alkaline protease from Aspergillus oryzae: esterase activity
Biochim. Biophys. Acta
268
225-232
1972
Aspergillus oryzae
brenda
Danno, G.
Inhibitory effect of alcohols on esterolytic activity of proteinase from Aspergillus Sulphureus
Agric. Biol. Chem.
37
445-446
1973
Aspergillus sulphureus
-
brenda
Toepfer, H.; Piesche, K.
Characterization of alkaline protease from Aspergillus ochraceus
Folia Haematol. Int. Mag. Klin. Morphol. Blutforsch.
101
91-98
1974
Aspergillus ochraceus
brenda
Lai, T.S.; Chang, Y.K.
Isolation, purification, and substrate specificity of the alkaline proteinase of Aspergillus sojae
J. Chin. Biochem. Soc.
1
61-71
1972
Aspergillus sojae, Aspergillus sojae NTU-163
-
brenda
Turkova, J.; Mikes, O.
Reinvestigation of molecular weight of alkaline proteinase from Aspergillus flavus
Collect. Czech. Chem. Commun.
37
1408-1411
1972
Aspergillus flavus
-
brenda
Shih, I.L.; Chiu, L.C.; Lai, C.T.; Liaw, W.C.; Tai, D.F.
Enzymes catalyzed esterification of N-protcted amino acids with secondary alcohol
Biotechnol. Lett.
19
857-859
1997
Aspergillus oryzae
-
brenda
Samarntarn, W.; Cheevadhanarak, S.; Tanticharoen, M.
Production of alkaline protease by a genetically engineered Aspergillus oryzae U1521
J. Gen. Appl. Microbiol.
45
99-103
1999
Aspergillus oryzae, Aspergillus oryzae U152
brenda
te Biesebeke, R.; Record, E.; van Biezen, N.; Heerikhuisen, M.; Franken, A.; Punt, P.J.; van den Hondel, C.A.
Branching mutants of Aspergillus oryzae with improved amylase and protease production on solid substrates
Appl. Microbiol. Biotechnol.
69
44-50
2005
Aspergillus oryzae
brenda
Nehra, K.S.; Singh, A.; Sharma, J.; Kumar, R.; Dhillon, S.
Production and characterization of alkaline protease from Aspergillus sp. and its compatibility with commercial detergents
Asian J. Microbiol. Biotechnol. Environ. Sci.
6
67-72
2004
Aspergillus sp.
-
brenda
Tremacoldi, C.R.; Carmona, E.C.
Production of extracellular alkaline proteases by Aspergillus clavatus
World J. Microbiol. Biotechnol.
21
169-172
2005
Aspergillus clavatus
-
brenda
Miyazawa, T.; Imagawa, K.; Yamada, T.
Use of Aspergillus oryzae protease for the resolution of alpha-hydroxy acids by enantioselective ester hydrolysis
Biocatal. Biotransform.
24
291-298
2006
Aspergillus oryzae
-
brenda
te Biesebeke, R.; Boussier, A.; van Biezen, N.; Braaksma, M.; van den Hondel, C.A.; de Vos, W.M.; Punt, P.J.
Expression of Aspergillus hemoglobin domain activities in Aspergillus oryzae grown on solid substrates improves growth rate and enzyme production
Biotechnol. J.
1
822-827
2006
Aspergillus oryzae, Aspergillus oryzae ATCC 16168
brenda
Pereira, J.L.; Franco, O.L.; Noronha, E.F.
Production and biochemical characterization of insecticidal enzymes from Aspergillus fumigatus toward Callosobruchus maculatus
Curr. Microbiol.
52
430-434
2006
Aspergillus fumigatus
brenda
Babu, I.S.; Srinubabu, G.; Kumar, N.K.; Kumari, K.S.; Yugandhar, M.N.; Raju, C.A.
Response surface optimization of critical medium components for the production of alkaline protease by Aspergillus foetidus
Int. J. Chem. Sci.
4
951-958
2006
Aspergillus foetidus, Aspergillus foetidus NCIM637
-
brenda
Sharma, J.; Singh, A.; Kumar, R.; Mittal, A.
Partial purification of an alkaline protease from a new strain of Aspergillus oryzae AWT 20 and its enhanced stabilization in entrapped Ca-alginate beads
Internet J. Microbiol.
2
0000
2006
Aspergillus oryzae, Aspergillus oryzae AWT20
-
brenda
Guo, J.P.; Ma, Y.
High-level expression, purification and characterization of recombinant Aspergillus oryzae alkaline protease in Pichia pastoris
Protein Expr. Purif.
58
301-308
2008
Aspergillus oryzae (P12547), Aspergillus oryzae RIB 40 (P12547)
brenda
Yadav, S.; Bisht, D.; Shikh, S.; Darmwal, N.
Oxidant and solvent stable alkaline protease from Aspergillus flavus and its characterization
Afr. J. Biotechnol.
10
8630-8640
2011
Aspergillus flavus, Aspergillus flavus MTCC 9952
-
brenda
Morya, V.; Yadav, S.; Kim, E.; Yadav, D.
In silico characterization of alkaline proteases from different species of Aspergillus
Appl. Biochem. Biotechnol.
166
243-257
2012
Aspergillus clavatus (A1CIA7), Aspergillus clavatus, Aspergillus flavus (B8N106), Aspergillus flavus (P35211), Aspergillus oryzae (P12547), Aspergillus oryzae, Aspergillus flavus ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167 (B8N106), Aspergillus clavatus ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 (A1CIA7), Aspergillus oryzae RIB 40 (P12547)
brenda
Behnsen, J.; Lessing, F.; Schindler, S.; Wartenberg, D.; Jacobsen, I.D.; Thoen, M.; Zipfel, P.F.; Brakhage, A.A.
Secreted Aspergillus fumigatus protease Alp1 degrades human complement proteins C3, C4, and C5
Infect. Immun.
78
3585-3594
2010
Aspergillus fumigatus, Aspergillus fumigatus DELTAakuBKU80
brenda
Castro-Ochoa, D.; Pena-Montes, C.; Farres, A.
Evaluation of strategies to improve the production of alkaline protease PrtA from Aspergillus nidulans
Appl. Biochem. Biotechnol.
169
1672-1682
2013
Aspergillus nidulans, Aspergillus nidulans PW1
brenda
Syed, R.; Rani, R.; Sabeena, R.; Masoodi, T.A.; Shafi, G.; Alharbi, K.
Functional analysis and structure determination of alkaline protease from Aspergillus flavus
Bioinformation
8
175-180
2012
Aspergillus flavus
brenda
Morais, H.; Silvestre, M.; Silveira, J.; Silva, A.; Silva, V.; Silva, M.
Action of a pancreatin and an Aspergillus oryzae protease on whey proteins: correlation among the methods of analysis of the enzymatic hydrolysates
Braz. Arch. Biol. Technol.
56
985-995
2013
Aspergillus oryzae
-
brenda
Ke, Y.; Huang, W.Q.; Li, J.Z.; Xie, M.Q.; Luo, X.C.
Enzymatic characteristics of a recombinant neutral protease I (rNpI) from Aspergillus oryzae expressed in Pichia pastoris
J. Agric. Food Chem.
60
12164-12169
2012
Aspergillus oryzae
brenda
Selvam, R.M.; Nithya, R.; Devi, P.N.; Shree, R.S.; Nila, M.V.; Demonte, N.L.; Thangavel, C.; Maheshwari, J.J.; Lalitha, P.; Prajna, N.V.; Dharmalingam, K.
Exoproteome of Aspergillus flavus corneal isolates and saprophytes: Identification of proteoforms of an oversecreted alkaline protease
J. Proteomics
115
23-35
2015
Aspergillus flavus
brenda
Niyonzima, F.N.; More, S.S.
Purification and characterization of detergent-compatible protease from Aspergillus terreus gr
3 Biotech
5
61-70
2015
Aspergillus terreus
brenda
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
Int. J. Biol. Macromol.
109
1039-1044
2018
Aspergillus tamarii, Aspergillus tamarii URM4634
brenda
Abdel Wahab, W.A.; Ahmed, S.A.
Response surface methodology for production, characterization and application of solvent, salt and alkali-tolerant alkaline protease from isolated fungal strain Aspergillus niger WA 2017
Int. J. Biol. Macromol.
115
447-458
2018
Aspergillus niger, Aspergillus niger WA 2017
brenda
Salihi, A.; Asoodeh, A.; Aliabadian, M.
Production and biochemical characterization of an alkaline protease from Aspergillus oryzae CH93
Int. J. Biol. Macromol.
94
827-835
2017
Aspergillus oryzae, Aspergillus oryzae CH93
brenda
Yilmaz, B.; Baltaci, M.O.; Sisecioglu, M.; Adiguzel, A.
Thermotolerant alkaline protease enzyme from Bacillus licheniformis A10 purification, characterization, effects of surfactants and organic solvents
J. Enzyme Inhib. Med. Chem.
31
1241-1247
2016
Bacillus licheniformis, Bacillus licheniformis A10
brenda
Xin, Y.; Sun, Z.; Chen, Q.; Wang, J.; Wang, Y.; Luogong, L.; Li, S.; Dong, W.; Cui, Z.; Huang, Y.
Purification and characterization of a novel extracellular thermostable alkaline protease from Streptomyces sp. M30
J. Microbiol. Biotechnol.
25
1944-1953
2015
Streptomyces sp. M30 (A0A0C4XY83)
brenda
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
J. Sci. Food. Agric.
99
3359-3366
2019
Aspergillus oryzae, Aspergillus oryzae 3.042
brenda
Ida, E.L.; da Silva, R.R.; de Oliveira, T.B.; Souto, T.B.; Leite, J.A.; Rodrigues, A.; Cabral, H.
Biochemical properties and evaluation of washing performance in commercial detergent compatibility of two collagenolytic serine peptidases secreted by Aspergillus fischeri and Penicillium citrinum
Prep. Biochem. Biotechnol.
47
282-290
2017
Aspergillus fischeri (A1CZ35), Penicillium citrinum (Q9Y749), Aspergillus fischeri FGSC A1164 (A1CZ35), Aspergillus fischeri ATCC 1020 (A1CZ35), Aspergillus fischeri JCM 1740 (A1CZ35), Aspergillus fischeri CBS 544.65 (A1CZ35), Aspergillus fischeri WB 181 (A1CZ35), Aspergillus fischeri DSM 3700 (A1CZ35)
brenda
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
Protein Expr. Purif.
148
24-29
2018
Aspergillus sojae (A0A386IRJ1), Aspergillus sojae GIM3.33 (A0A386IRJ1)
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