DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
Aspergillus awamori
DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
Aspergillus fumigatus
gene apnS, DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus, expression of the proenzyme in Saccharomyces cerevisiae, and in Escherichia coli inclusion bodies, expression of the N-terminal sequence in Escherichia coli
Aspergillus phoenicis
gene pepA, located on chromosome 1, DNA and amino acid sequence determination and analysis, genetic organization, phylogenetic analysis of Aspergillus
Aspergillus niger
proctase B, DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
Aspergillus oryzae
chymotrypsinogen A + H2O
Aspergillus phoenicis
activation
chymotrypsin + peptide fragment
?
chymotrypsinogen A + H2O
Aspergillus phoenicis R-3813
activation
chymotrypsin + peptide fragment
?
DRVYIHPFHLLVYS + 3 H2O
Aspergillus oryzae
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVY + Ile-His + PFHLL + VYS
?
DRVYIHPFHLLVYS + 3 H2O
Aspergillus sojae
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVY + Ile-His + PFHLL + VYS
?
DRVYIHPFHLLVYS + 3 H2O
Aspergillus phoenicis
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVY + Ile-His + PFHLL + Val-Tyr-Ser
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 3 H2O
Aspergillus sojae
substrate is the oxidized insulin B chain, primarily cleavage at Leu15-Tyr16 and Phe24-Phe25, and minor cleavage of Tyr16-Leu17, overview
FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA
?
additional information
Aspergillus fumigatus
the extracellular enzyme pays a role in development of aspergillosis in lung of mammalia, but it is not essential for virulence
?
proangiotensin + H2O
Aspergillus phoenicis
the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVYIH + PFHLLVYS
i.e. angiotensin I
?
trypsinogen + H2O
Aspergillus phoenicis
activation by cleavage of a Lys-Pro bond
trypsin + peptide fragment
?
casein + H2O
milk casein
668812
Aspergillus phoenicis
?
?
casein + H2O
milk casein
668812
Aspergillus phoenicis R-3813
?
?
chymotrypsinogen A + H2O
activation
668812
Aspergillus phoenicis
chymotrypsin + peptide fragment
?
chymotrypsinogen A + H2O
activation
668812
Aspergillus phoenicis R-3813
chymotrypsin + peptide fragment
?
Dnp-Ala-Ala-Phe-Phe-Ala-Arg-NH2 + H2O
chromogenic synthetic peptide substrate
668812
Aspergillus phoenicis
Dnp-Ala-Ala-Phe + Phe-Ala-Arg-NH2
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus oryzae
DRVY + Ile-His + PFHLL + VYS
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis
DRVY + Ile-His + PFHLL + VYS
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus sojae
DRVY + Ile-His + PFHLL + VYS
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis R-3813
DRVY + Ile-His + PFHLL + VYS
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis
DRVY + Ile-His + PFHLL + Val-Tyr-Ser
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 3 H2O
substrate is the oxidized insulin B chain, primarily cleavage at Leu15-Tyr16 and Phe24-Phe25, and minor cleavage of Tyr16-Leu17, overview
668812
Aspergillus sojae
FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
substrate is the oxidized insulin B chain, cleavage site specificity, overview
668812
Aspergillus phoenicis
FVNQHLCGSH + LVEA + Leu + Tyr + LVCGERGF + FYTPKA
?
additional information
the extracellular enzyme pays a role in development of aspergillosis in lung of mammalia, but it is not essential for virulence
668812
Aspergillus fumigatus
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus niger
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus oryzae
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus phoenicis
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus sojae
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus awamori
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus kawachii
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus foetidus
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys, at pH 5.5 the enzyme shows also an elastolytic activity with elastin Congo red
668812
Aspergillus fumigatus
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys, no activity with Z-Glu-Tyr or Z-Tyr-Leu, no milk clotting
668812
Aspergillus phoenicis
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus phoenicis R-3813
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys, no activity with Z-Glu-Tyr or Z-Tyr-Leu, no milk clotting
668812
Aspergillus phoenicis R-3813
?
proangiotensin + H2O
the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis
DRVYIH + PFHLLVYS
i.e. angiotensin I
?
trypsinogen + H2O
activation by cleavage of a Lys-Pro bond
668812
Aspergillus phoenicis
trypsin + peptide fragment
?
Acid protease
Aspergillus oryzae
Aspartic proteinase
Aspergillus oryzae
Aspartic proteinase
Aspergillus phoenicis
Aspartic proteinase
Aspergillus sojae
aspergillopepsin
Aspergillus foetidus
Aspergillopepsin A
Aspergillus awamori
Aspergillopepsin A
Aspergillus niger
Aspergillopepsin F
Aspergillus fumigatus
aspergillopepsin O
Aspergillus oryzae
Aspergillopeptidase A
Aspergillus phoenicis
Awamorin
Aspergillus awamori
carboxyl protease
Aspergillus kawachii
carboxyl proteinase I
Aspergillus sojae
extracellular aspartic protease
Aspergillus fumigatus
extracellular aspartic protease
Aspergillus niger
More
the enzyme belongs to the A1 peptidase family
Aspergillus awamori
More
the enzyme belongs to the A1 peptidase family
Aspergillus foetidus
More
the enzyme belongs to the A1 peptidase family
Aspergillus fumigatus
More
the enzyme belongs to the A1 peptidase family
Aspergillus kawachii
More
the enzyme belongs to the A1 peptidase family
Aspergillus niger
More
the enzyme belongs to the A1 peptidase family
Aspergillus oryzae
More
the enzyme belongs to the A1 peptidase family
Aspergillus phoenicis
More
the enzyme belongs to the A1 peptidase family
Aspergillus sojae
Proctase B
Aspergillus niger
Proteinase B
Aspergillus niger
DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
Aspergillus awamori
DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
Aspergillus fumigatus
gene apnS, DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus, expression of the proenzyme in Saccharomyces cerevisiae, and in Escherichia coli inclusion bodies, expression of the N-terminal sequence in Escherichia coli
Aspergillus phoenicis
gene pepA, located on chromosome 1, DNA and amino acid sequence determination and analysis, genetic organization, phylogenetic analysis of Aspergillus
Aspergillus niger
proctase B, DNA and amino acid sequence determination and analysis, phylogenetic analysis of Aspergillus
Aspergillus oryzae
chymotrypsinogen A + H2O
Aspergillus phoenicis
activation
chymotrypsin + peptide fragment
?
chymotrypsinogen A + H2O
Aspergillus phoenicis R-3813
activation
chymotrypsin + peptide fragment
?
DRVYIHPFHLLVYS + 3 H2O
Aspergillus oryzae
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVY + Ile-His + PFHLL + VYS
?
DRVYIHPFHLLVYS + 3 H2O
Aspergillus sojae
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVY + Ile-His + PFHLL + VYS
?
DRVYIHPFHLLVYS + 3 H2O
Aspergillus phoenicis
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVY + Ile-His + PFHLL + Val-Tyr-Ser
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 3 H2O
Aspergillus sojae
substrate is the oxidized insulin B chain, primarily cleavage at Leu15-Tyr16 and Phe24-Phe25, and minor cleavage of Tyr16-Leu17, overview
FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA
?
additional information
Aspergillus fumigatus
the extracellular enzyme pays a role in development of aspergillosis in lung of mammalia, but it is not essential for virulence
?
proangiotensin + H2O
Aspergillus phoenicis
the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
DRVYIH + PFHLLVYS
i.e. angiotensin I
?
trypsinogen + H2O
Aspergillus phoenicis
activation by cleavage of a Lys-Pro bond
trypsin + peptide fragment
?
casein + H2O
milk casein
668812
Aspergillus phoenicis
?
?
casein + H2O
milk casein
668812
Aspergillus phoenicis R-3813
?
?
chymotrypsinogen A + H2O
activation
668812
Aspergillus phoenicis
chymotrypsin + peptide fragment
?
chymotrypsinogen A + H2O
activation
668812
Aspergillus phoenicis R-3813
chymotrypsin + peptide fragment
?
Dnp-Ala-Ala-Phe-Phe-Ala-Arg-NH2 + H2O
chromogenic synthetic peptide substrate
668812
Aspergillus phoenicis
Dnp-Ala-Ala-Phe + Phe-Ala-Arg-NH2
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus oryzae
DRVY + Ile-His + PFHLL + VYS
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis
DRVY + Ile-His + PFHLL + VYS
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus sojae
DRVY + Ile-His + PFHLL + VYS
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis R-3813
DRVY + Ile-His + PFHLL + VYS
?
DRVYIHPFHLLVYS + 3 H2O
tetradecapeptide renin substrate, the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis
DRVY + Ile-His + PFHLL + Val-Tyr-Ser
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + 3 H2O
substrate is the oxidized insulin B chain, primarily cleavage at Leu15-Tyr16 and Phe24-Phe25, and minor cleavage of Tyr16-Leu17, overview
668812
Aspergillus sojae
FVNQHLCGSHLVEAL + Tyr + LVCGERGF + FYTPKA
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
substrate is the oxidized insulin B chain, cleavage site specificity, overview
668812
Aspergillus phoenicis
FVNQHLCGSH + LVEA + Leu + Tyr + LVCGERGF + FYTPKA
?
additional information
the extracellular enzyme pays a role in development of aspergillosis in lung of mammalia, but it is not essential for virulence
668812
Aspergillus fumigatus
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus niger
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus oryzae
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus phoenicis
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus sojae
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus awamori
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus kawachii
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus foetidus
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys, at pH 5.5 the enzyme shows also an elastolytic activity with elastin Congo red
668812
Aspergillus fumigatus
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys, no activity with Z-Glu-Tyr or Z-Tyr-Leu, no milk clotting
668812
Aspergillus phoenicis
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys
668812
Aspergillus phoenicis R-3813
?
additional information
the enzyme prefers hydrophobic amino acid residues at P1 and P1', but also accepts Lys, no activity with Z-Glu-Tyr or Z-Tyr-Leu, no milk clotting
668812
Aspergillus phoenicis R-3813
?
proangiotensin + H2O
the enzyme cleaves the Xaa-pro bond with Xaa being any amino acid
668812
Aspergillus phoenicis
DRVYIH + PFHLLVYS
i.e. angiotensin I
?
trypsinogen + H2O
activation by cleavage of a Lys-Pro bond
668812
Aspergillus phoenicis
trypsin + peptide fragment
?
754972
Yoshiya
HAP-01, the first chromogenic ...
Aspergillus oryzae
Org. Biomol. Chem.
17
776-779
2019
-
-
-
-
-
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2
-
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2
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1
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2
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-
753450
Deng
Biocontrol activity of recomb ...
Trichoderma harzianum, Trichoderma harzianum GIM 3.442
Enzyme Microb. Technol.
112
35-42
2018
-
-
1
-
-
-
2
-
-
6
-
-
-
17
-
-
1
-
-
-
-
-
2
1
1
1
1
1
-
1
1
1
-
-
-
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-
-
1
-
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-
-
2
-
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6
-
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1
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-
2
1
1
1
1
-
1
1
1
-
-
1
1
-
-
-
754865
Lim
-
Ginsenoside Rg1 exhibits anti ...
Aspergillus sp.
Nat. Prod. Commun.
13
415-418
2018
-
-
-
-
-
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1
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1
1
-
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-
755227
Liu
The high expression of Asperg ...
Aspergillus pseudoglaucus
Prep. Biochem. Biotechnol.
48
725-733
2018
-
-
1
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3
-
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1
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4
1
3
1
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1
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2
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1
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1
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4
1
1
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1
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2
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753407
Yu
-
Construction and application ...
Aspergillus niger
Electron. J. Biotechnol.
29
32-38
2017
-
-
1
-
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1
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1
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1
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754494
Takenaka
Heterologous expression and c ...
Aspergillus pseudoglaucus, Aspergillus pseudoglaucus MK82
J. Sci. Food Agric.
97
95-101
2017
-
-
1
-
-
1
4
-
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7
-
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1
-
-
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4
1
2
1
-
1
-
1
-
1
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1
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1
-
4
-
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1
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-
4
1
1
-
1
-
1
-
1
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-
-
-
-
754932
Yang
Consumption of an acid protea ...
Aspergillus oryzae, Aspergillus oryzae ATCC 42149, Aspergillus oryzae RIB 40
Nutr. Res.
44
60-66
2017
-
-
-
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8
-
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1
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1
1
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1
2
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1
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1
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1
1
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1
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1
-
-
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-
2
2
-
-
-
752341
Niyonzima
Purification and characteriza ...
Aspergillus terreus, Aspergillus terreus gr.
3 Biotech
5
61-70
2015
4
-
-
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-
1
17
-
-
4
-
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2
1
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1
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-
-
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1
3
1
-
1
-
1
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1
1
1
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4
-
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1
-
17
-
-
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4
-
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1
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1
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1
3
1
1
-
1
-
1
1
1
-
-
-
-
-
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-
753307
Namvar
-
Aspergillus fumigatus proteas ...
Aspergillus fumigatus, Aspergillus fumigatus A1160
Clin. Exp. Allergy
45
982-993
2015
-
-
-
-
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-
-
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2
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2
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2
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-
2
-
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-
-
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-
1
1
-
-
-
680281
Landbo
Protease-assisted clarificatio ...
Aspergillus niger
J. Agric. Food Chem.
54
6554-6563
2006
-
-
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1
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1
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1
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1
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-
-
668006
Zhu
Analysis of secreted proteins ...
Aspergillus oryzae, Aspergillus oryzae RIB 40
Biosci. Biotechnol. Biochem.
68
2607-2612
2004
-
-
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1
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1
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2
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5
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1
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1
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2
4
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1
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1
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1
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1
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2
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668812
Ichishima
-
Aspergillopepsin I ...
Aspergillus awamori, Aspergillus foetidus, Aspergillus fumigatus, Aspergillus kawachii, Aspergillus niger, Aspergillus oryzae, Aspergillus phoenicis, Aspergillus phoenicis R-3813, Aspergillus sojae
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
92-99
2004
-
5
5
1
1
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1
-
8
-
2
9
-
10
-
1
1
1
1
9
-
-
26
6
27
-
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-
4
1
1
-
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-
5
5
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Purification and characterizat ...
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Iio
Specificity of acid proteinase ...
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Davidson
Aspergillus oryzae acid protei ...
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30566
Morihara
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Kovaleva
The site of diazoacetyl inhibi ...
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Ichishima
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Purification and mode of assay ...
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3
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2
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