BRENDA - Enzyme Database show
show all sequences of 3.4.21.63

Enzymatic characteristics of a recombinant neutral protease I (rNpI) from Aspergillus oryzae expressed in Pichia pastoris

Ke, Y.; Huang, W.Q.; Li, J.Z.; Xie, M.Q.; Luo, X.C.; J. Agric. Food Chem. 60, 12164-12169 (2012)

Data extracted from this reference:

Application
Application
Commentary
Organism
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
Aspergillus oryzae
Cloned(Commentary)
Commentary
Organism
recombinant expression of a truncated neutral protease I in Pichia pastoris with a high enzyme yield
Aspergillus oryzae
Inhibitors
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Aspergillus oryzae
EDTA
-
Aspergillus oryzae
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
the enzyme has a zinc-binding motif and is a gluzincin
Aspergillus oryzae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aspergillus oryzae
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
731961
Aspergillus oryzae
?
-
-
-
-
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
731961
Aspergillus oryzae
?
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
55
-
recombinant enzyme
Aspergillus oryzae
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
purified recombinant truncated neutral protease I, 120 min, over 90% activity remaining
Aspergillus oryzae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
recombinant enzyme
Aspergillus oryzae
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
5
9
purified recombinant truncated neutral protease I, stable at
Aspergillus oryzae
Application (protein specific)
Application
Commentary
Organism
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
Aspergillus oryzae
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of a truncated neutral protease I in Pichia pastoris with a high enzyme yield
Aspergillus oryzae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cu2+
-
Aspergillus oryzae
EDTA
-
Aspergillus oryzae
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
the enzyme has a zinc-binding motif and is a gluzincin
Aspergillus oryzae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
731961
Aspergillus oryzae
?
-
-
-
-
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
731961
Aspergillus oryzae
?
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
55
-
recombinant enzyme
Aspergillus oryzae
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
purified recombinant truncated neutral protease I, 120 min, over 90% activity remaining
Aspergillus oryzae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
recombinant enzyme
Aspergillus oryzae
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
5
9
purified recombinant truncated neutral protease I, stable at
Aspergillus oryzae
General Information
General Information
Commentary
Organism
evolution
the enzyme belongs to the gluzincin family
Aspergillus oryzae
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme belongs to the gluzincin family
Aspergillus oryzae
Other publictions for EC 3.4.21.63
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
732387
Selvam
Exoproteome of Aspergillus fla ...
Aspergillus flavus
J. Proteomics
115
23-35
2015
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1
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731156
Castro-Ochoa
Evaluation of strategies to im ...
Aspergillus nidulans, Aspergillus nidulans PW1
Appl. Biochem. Biotechnol.
169
1672-1682
2013
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1
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1
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731567
Morais
-
Action of a pancreatin and an ...
Aspergillus oryzae
Braz. Arch. Biol. Technol.
56
985-995
2013
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1
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717111
Morya
In silico characterization of ...
Aspergillus clavatus, Aspergillus clavatus ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1, Aspergillus flavus, Aspergillus flavus ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167, Aspergillus oryzae, Aspergillus oryzae RIB 40
Appl. Biochem. Biotechnol.
166
243-257
2012
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3
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13
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731392
Syed
Functional analysis and struct ...
Aspergillus flavus
Bioinformation
8
175-180
2012
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731961
Ke
Enzymatic characteristics of a ...
Aspergillus oryzae
J. Agric. Food Chem.
60
12164-12169
2012
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1
1
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1
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6
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717055
Yadav
-
Oxidant and solvent stable alk ...
Aspergillus flavus, Aspergillus flavus MTCC 9952
Afr. J. Biotechnol.
10
8630-8640
2011
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1
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7
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1
4
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11
2
1
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4
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7
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4
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11
1
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1
1
4
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1
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1
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1
1
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717658
Behnsen
Secreted Aspergillus fumigatus ...
Aspergillus fumigatus, Aspergillus fumigatus DELTAakuBKU80
Infect. Immun.
78
3585-3594
2010
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1
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682690
Guo
High-level expression, purific ...
Aspergillus oryzae, Aspergillus oryzae RIB 40
Protein Expr. Purif.
58
301-308
2008
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1
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9
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2
1
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1
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9
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2
1
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1
1
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677898
Miyazawa
-
Use of Aspergillus oryzae prot ...
Aspergillus oryzae
Biocatal. Biotransform.
24
291-298
2006
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678860
te Biesebeke
Expression of Aspergillus hemo ...
Aspergillus oryzae, Aspergillus oryzae ATCC 16168
Biotechnol. J.
1
822-827
2006
1
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679374
Pereira
Production and biochemical cha ...
Aspergillus fumigatus
Curr. Microbiol.
52
430-434
2006
1
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680223
Babu
-
Response surface optimization ...
Aspergillus foetidus, Aspergillus foetidus NCIM637
Int. J. Chem. Sci.
4
951-958
2006
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680260
Sharma
-
Partial purification of an alk ...
Aspergillus oryzae, Aspergillus oryzae AWT20
Internet J. Microbiol.
2
0000
2006
1
1
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8
1
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2
1
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2
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667281
te Biesebeke
Branching mutants of Aspergill ...
Aspergillus oryzae
Appl. Microbiol. Biotechnol.
69
44-50
2005
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671008
Tremacoldi
-
Production of extracellular al ...
Aspergillus clavatus
World J. Microbiol. Biotechnol.
21
169-172
2005
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667362
Nehra
-
Production and characterizatio ...
Aspergillus sp.
Asian J. Microbiol. Biotechnol. Environ. Sci.
6
67-72
2004
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652661
Samarntarn
Production of alkaline proteas ...
Aspergillus oryzae, Aspergillus oryzae U152
J. Gen. Appl. Microbiol.
45
99-103
1999
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650680
Shih
-
Enzymes catalyzed esterificati ...
Aspergillus oryzae
Biotechnol. Lett.
19
857-859
1997
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29493
Ogundero
The purification and activitie ...
Aspergillus clavatus
J. Basic Microbiol.
26
241-248
1986
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29488
Impoolsup
Isolation of alkaline and neut ...
Aspergillus flavus
Appl. Environ. Microbiol.
42
619-628
1981
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29492
Nakatani
Interaction of Asp. melleus Se ...
Aspergillus melleus
J. Biochem.
81
1269-1272
1977
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1
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1
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29491
Kundu
Purification and characterizat ...
Aspergillus oryzae, Aspergillus oryzae EI212
Appl. Microbiol.
30
507-513
1975
1
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1
6
1
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1
1
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2
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1
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1
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6
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1
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1
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1
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6
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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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6
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1
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29482
Spadari
Highly restricted specificity ...
Aspergillus oryzae
Biochim. Biophys. Acta
359
267-272
1974
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2
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29483
Morihara
Comparative study of various s ...
Aspergillus melleus, Aspergillus sojae
Arch. Biochem. Biophys.
165
72-79
1974
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2
13
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2
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30
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8
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2
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13
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30
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8
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29498
Toepfer
Characterization of alkaline p ...
Aspergillus ochraceus
Folia Haematol. Int. Mag. Klin. Morphol. Blutforsch.
101
91-98
1974
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1
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1
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1
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4
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1
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1
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4
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29489
Nakadai
-
Purification and properties of ...
Aspergillus oryzae
Agric. Biol. Chem.
37
2685-2694
1973
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3
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1
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1
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1
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1
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5
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5
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1
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3
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1
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1
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1
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5
-
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5
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1
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29490
Danno
-
Substrate specificity of alkal ...
Aspergillus sulphureus, Aspergillus sydowii
Agric. Biol. Chem.
37
1493-1496
1973
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2
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4
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4
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29494
Feinstein
Isolation of alkaline proteina ...
Aspergillus oryzae
Biochim. Biophys. Acta
309
196-202
1973
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3
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3
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3
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1
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3
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3
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29495
Klapper
The purification and propertie ...
Aspergillus oryzae, Aspergillus oryzae NRRL 2160
Biochim. Biophys. Acta
304
505-512
1973
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3
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1
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1
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2
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1
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4
1
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2
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3
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1
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1
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1
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4
1
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2
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29497
Danno
-
Inhibitory effect of alcohols ...
Aspergillus sulphureus
Agric. Biol. Chem.
37
445-446
1973
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4
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1
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4
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29481
Turkova
Alkaline proteinases of the ge ...
Aspergillus oryzae, Aspergillus sojae, Aspergillus sulphureus
Biochim. Biophys. Acta
257
257-263
1972
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3
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3
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3
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3
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3
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29485
Hayashi
-
Some characteristics of hydrol ...
Aspergillus sojae
Agric. Biol. Chem.
36
1755-1765
1972
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1
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10
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10
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29486
Nasuno
-
Purification of alkaline prote ...
Aspergillus candidus
Agric. Biol. Chem.
36
1791-1796
1972
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2
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1
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2
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1
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1
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2
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29487
Ohara
-
Enzymic properties of alkaline ...
Aspergillus candidus
Agric. Biol. Chem.
36
1797-1802
1972
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1
15
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1
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1
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1
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3
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1
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2
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3
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1
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15
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1
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1
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3
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1
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2
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3
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29496
Ku
Alkaline protease from Aspergi ...
Aspergillus oryzae
Biochim. Biophys. Acta
268
225-232
1972
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1
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1
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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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1
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29499
Lai
-
Isolation, purification, and s ...
Aspergillus sojae, Aspergillus sojae NTU-163
J. Chin. Biochem. Soc.
1
61-71
1972
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1
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2
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1
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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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4
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1
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1
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29500
Turkova
-
Reinvestigation of molecular w ...
Aspergillus flavus
Collect. Czech. Chem. Commun.
37
1408-1411
1972
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2
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1
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1
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2
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1
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29484
Nakagawa
-
Alkaline proteinases from Aspe ...
Aspergillus flavus, Aspergillus oryzae, Aspergillus sojae, Aspergillus sydowii
Methods Enzymol.
19
581-591
1970
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11
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4
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2
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4
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2
1
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2
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4
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2
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2
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1
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11
-
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4
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2
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2
1
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2
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4
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2
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2
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1
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