BRENDA - Enzyme Database
show all sequences of 1.1.5.9

Characterization of different FAD-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells

Zafar, M.N.; Beden, N.; Leech, D.; Sygmund, C.; Ludwig, R.; Gorton, L.; Anal. Bioanal. Chem. 402, 2069-2077 (2012)

Data extracted from this reference:

Application
Application
Commentary
Organism
analysis
possible use of the enzyme as amperometric glucose biosensor
Aspergillus sp.
analysis
possible use of the enzyme as amperometric glucose biosensor
Colletotrichum gloeosporioides
analysis
possible use of the enzyme as amperometric glucose biosensor
Komagataella pastoris
Cloned(Commentary)
Commentary
Organism
recombinant expression in Pichia pastoris
Colletotrichum gloeosporioides
Engineering
Amino acid exchange
Commentary
Organism
additional information
the FAD-dependent glucose dehydrogenase is evaluated electrochemically connected to an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+ on graphite electrode for possible use in glucose-based biosensors and biofuel cells, method and sensitivity, overview
Aspergillus sp.
additional information
the FAD-dependent glucose dehydrogenase is evaluated electrochemically connected to an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+ on graphite electrode for possible use in glucose-based biosensors and biofuel cells, method and sensitivity, overview
Colletotrichum gloeosporioides
additional information
the FAD-dependent glucose dehydrogenase is evaluated electrochemically connected to an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+ on graphite electrode for possible use in glucose-based biosensors and biofuel cells, method and sensitivity, overview
Komagataella pastoris
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
67000
-
x * 67000, deglycosylated recombinant enzyme, SDS-PAGE
Aspergillus sp.
88000
131000
-
Komagataella pastoris
95000
135000
recombinant enzyme
Colletotrichum gloeosporioides
97000
-
deglycosylated enzyme, gel filtration
Aspergillus sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose + a quinone
Komagataella pastoris
-
D-glucono-1,5-lactone + a quinol
-
-
?
D-glucose + a quinone
Colletotrichum gloeosporioides
-
D-glucono-1,5-lactone + a quinol
-
-
?
D-glucose + a quinone
Aspergillus sp.
-
D-glucono-1,5-lactone + a quinol
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aspergillus sp.
-
-
-
Colletotrichum gloeosporioides
-
-
-
Komagataella pastoris
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
glycoprotein
-
Aspergillus sp.
glycoprotein
-
Komagataella pastoris
glycoprotein
-
Colletotrichum gloeosporioides
Source Tissue
Source Tissue
Commentary
Organism
Textmining
commercial preparation
-
Aspergillus sp.
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
795
-
pH and temperature not specified in the publication
Aspergillus sp.
836
-
pH and temperature not specified in the publication
Komagataella pastoris
878
-
pH and temperature not specified in the publication
Colletotrichum gloeosporioides
Storage Stability
Storage Stability
Organism
GcGDH/Os-polymer modified electrode under storage conditions of 50 mM phosphate buffer, pH 7.4, 4 °C, injection of 0.05 ml of a 5 mM glucose solution into the electrochemical cell for 6 days, the biosensor keeps more than 90% of its initial activity after the first day
Colletotrichum gloeosporioides
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-deoxy-D-glucose + a quinone
-
723928
Colletotrichum gloeosporioides
2-deoxy-D-glucono-1,5-lactone + a quinol
-
-
-
?
cellobiose + a quinone
low activity
723928
Colletotrichum gloeosporioides
? + a quinol
-
-
-
?
D-glucose + a quinone
-
723928
Komagataella pastoris
D-glucono-1,5-lactone + a quinol
-
-
-
?
D-glucose + a quinone
-
723928
Colletotrichum gloeosporioides
D-glucono-1,5-lactone + a quinol
-
-
-
?
D-glucose + a quinone
-
723928
Aspergillus sp.
D-glucono-1,5-lactone + a quinol
-
-
-
?
D-xylose + ferricenium ion
-
723928
Colletotrichum gloeosporioides
D-xylono-1,5-lactone + ferrocenium ion
-
-
-
?
glutamine + a quinone
low activity
723928
Colletotrichum gloeosporioides
? + a quinol
-
-
-
?
additional information
substrate specificity, overview. Lactose, gluconic acid, mannose, mannitol, sorbitol, galactose, sucrose, maltose, arabinose, xylitol, rhamnose, fucose, trehalose, and fructose are poor or no substrates
723928
Colletotrichum gloeosporioides
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 67000, deglycosylated recombinant enzyme, SDS-PAGE
Aspergillus sp.
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
dependent on
Aspergillus sp.
FAD
dependent on
Komagataella pastoris
FAD
dependent on
Colletotrichum gloeosporioides
Application (protein specific)
Application
Commentary
Organism
analysis
possible use of the enzyme as amperometric glucose biosensor
Aspergillus sp.
analysis
possible use of the enzyme as amperometric glucose biosensor
Colletotrichum gloeosporioides
analysis
possible use of the enzyme as amperometric glucose biosensor
Komagataella pastoris
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression in Pichia pastoris
Colletotrichum gloeosporioides
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
dependent on
Aspergillus sp.
FAD
dependent on
Komagataella pastoris
FAD
dependent on
Colletotrichum gloeosporioides
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
the FAD-dependent glucose dehydrogenase is evaluated electrochemically connected to an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+ on graphite electrode for possible use in glucose-based biosensors and biofuel cells, method and sensitivity, overview
Aspergillus sp.
additional information
the FAD-dependent glucose dehydrogenase is evaluated electrochemically connected to an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+ on graphite electrode for possible use in glucose-based biosensors and biofuel cells, method and sensitivity, overview
Colletotrichum gloeosporioides
additional information
the FAD-dependent glucose dehydrogenase is evaluated electrochemically connected to an osmium redox polymer [Os(4,4'-dimethyl-2,2'-bipyridine)2 (PVI)10Cl]+ on graphite electrode for possible use in glucose-based biosensors and biofuel cells, method and sensitivity, overview
Komagataella pastoris
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
67000
-
x * 67000, deglycosylated recombinant enzyme, SDS-PAGE
Aspergillus sp.
88000
131000
-
Komagataella pastoris
95000
135000
recombinant enzyme
Colletotrichum gloeosporioides
97000
-
deglycosylated enzyme, gel filtration
Aspergillus sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glucose + a quinone
Komagataella pastoris
-
D-glucono-1,5-lactone + a quinol
-
-
?
D-glucose + a quinone
Colletotrichum gloeosporioides
-
D-glucono-1,5-lactone + a quinol
-
-
?
D-glucose + a quinone
Aspergillus sp.
-
D-glucono-1,5-lactone + a quinol
-
-
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
glycoprotein
-
Aspergillus sp.
glycoprotein
-
Komagataella pastoris
glycoprotein
-
Colletotrichum gloeosporioides
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
commercial preparation
-
Aspergillus sp.
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
795
-
pH and temperature not specified in the publication
Aspergillus sp.
836
-
pH and temperature not specified in the publication
Komagataella pastoris
878
-
pH and temperature not specified in the publication
Colletotrichum gloeosporioides
Storage Stability (protein specific)
Storage Stability
Organism
GcGDH/Os-polymer modified electrode under storage conditions of 50 mM phosphate buffer, pH 7.4, 4 °C, injection of 0.05 ml of a 5 mM glucose solution into the electrochemical cell for 6 days, the biosensor keeps more than 90% of its initial activity after the first day
Colletotrichum gloeosporioides
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-deoxy-D-glucose + a quinone
-
723928
Colletotrichum gloeosporioides
2-deoxy-D-glucono-1,5-lactone + a quinol
-
-
-
?
cellobiose + a quinone
low activity
723928
Colletotrichum gloeosporioides
? + a quinol
-
-
-
?
D-glucose + a quinone
-
723928
Komagataella pastoris
D-glucono-1,5-lactone + a quinol
-
-
-
?
D-glucose + a quinone
-
723928
Colletotrichum gloeosporioides
D-glucono-1,5-lactone + a quinol
-
-
-
?
D-glucose + a quinone
-
723928
Aspergillus sp.
D-glucono-1,5-lactone + a quinol
-
-
-
?
D-xylose + ferricenium ion
-
723928
Colletotrichum gloeosporioides
D-xylono-1,5-lactone + ferrocenium ion
-
-
-
?
glutamine + a quinone
low activity
723928
Colletotrichum gloeosporioides
? + a quinol
-
-
-
?
additional information
substrate specificity, overview. Lactose, gluconic acid, mannose, mannitol, sorbitol, galactose, sucrose, maltose, arabinose, xylitol, rhamnose, fucose, trehalose, and fructose are poor or no substrates
723928
Colletotrichum gloeosporioides
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 67000, deglycosylated recombinant enzyme, SDS-PAGE
Aspergillus sp.
Other publictions for EC 1.1.5.9
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)
739924
Ozawa
Identification and characteriz ...
Rasamsonia emersonii, Rasamsonia emersonii NBRC 31232, Thermoascus crustaceus, Thermoascus crustaceus NBRC 9129
Appl. Microbiol. Biotechnol.
101
173-183
2017
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2
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-
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-
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2
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11
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2
2
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20
2
2
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2
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2
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2
2
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2
2
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2
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2
2
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20
2
2
-
2
-
2
-
2
-
-
-
-
-
-
-
740195
Sode
Novel fungal FAD glucose dehyd ...
Aspergillus niger
Biosens. Bioelectron.
87
305-311
2017
-
-
1
-
-
-
-
2
-
-
1
-
-
4
-
-
-
-
1
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3
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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3
1
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-
-
-
-
-
-
-
-
-
-
-
741496
Iwasa
-
Thermophilic Talaromyces emer ...
Rasamsonia emersonii
ACS Omega
2
1660-1665
2017
-
1
1
-
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-
-
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-
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1
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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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-
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741724
Ozawa
Identification and characteri ...
Rasamsonia emersonii, Thermoascus crustaceus, Thermoascus crustaceus NBRC 9129
Appl. Microbiol. Biotechnol.
101
173-183
2017
-
-
2
-
-
-
-
4
2
-
-
-
-
10
-
2
-
-
-
-
2
-
6
2
4
4
8
-
3
-
4
2
-
-
-
-
-
2
2
-
-
-
-
-
-
4
2
-
-
-
-
-
2
-
-
-
2
-
6
2
4
4
8
-
3
-
4
-
-
-
-
-
-
-
740120
Shiota
An Fe-S cluster in the conserv ...
Burkholderia cepacia
Bioelectrochemistry
112
178-183
2016
-
-
-
-
4
-
-
2
-
-
-
-
-
2
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
4
-
-
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-
2
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-
-
-
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-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
740363
Iwasa
-
Thermostable FAD-dependent glu ...
Thermoascus aurantiacus, Thermoascus aurantiacus NBRC 6766, Thermoascus aurantiacus NBRC 9748
Electrochemistry
84
342-348
2016
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
1
-
-
-
-
-
-
20
-
1
-
1
-
2
-
1
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
20
-
1
-
1
-
2
-
1
-
-
-
-
-
-
-
739817
Komori
Crystallographic analysis of F ...
Aspergillus terreus
Acta Crystallogr. Sect. F
71
1017-1019
2015
-
-
1
1
-
-
-
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
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-
1
-
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-
1
1
1
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-
-
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-
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-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
740224
Sakai
Stabilization of fungi-derived ...
Aspergillus flavus
Biotechnol. Lett.
37
1091-1099
2015
-
-
1
-
1
-
-
1
-
-
2
-
-
1
-
-
1
-
-
-
-
-
3
1
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-
1
2
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1
-
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1
1
-
1
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-
1
-
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2
-
-
-
-
1
-
-
-
-
3
1
-
-
1
2
-
-
-
-
-
-
-
-
1
1
740778
Satake
Novel glucose dehydrogenase fr ...
Mucor circinelloides, Mucor circinelloides NISL0103
J. Biosci. Bioeng.
120
498-503
2015
-
-
1
-
-
-
-
1
-
-
-
-
-
4
-
1
1
-
-
1
-
-
14
1
1
1
1
1
1
-
1
1
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
-
-
-
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1
1
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1
-
-
14
1
1
1
1
1
1
-
1
-
-
-
-
-
-
-
741412
Yoshida
Structural analysis of fungus- ...
Aspergillus flavus, Aspergillus flavus ATCC 200026
Sci. Rep.
5
13498
2015
-
-
1
1
2
-
-
-
-
-
-
-
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4
-
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1
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-
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2
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1
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1
1
1
2
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1
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2
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-
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740853
Yang
Efficient expression, purifica ...
Aspergillus terreus, Aspergillus terreus NIH2624
J. Microbiol. Biotechnol.
24
1516-1524
2014
-
-
1
-
-
-
-
1
-
-
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-
7
-
-
1
-
-
-
-
-
13
1
1
1
1
-
1
1
1
1
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
13
1
1
1
1
-
1
1
1
-
-
-
-
-
-
-
726109
Fapyane
High performance enzyme fuel c ...
Burkholderia cepacia
Phys. Chem. Chem. Phys.
15
9508-9512
2013
-
-
1
-
1
-
-
1
-
-
2
1
-
4
-
-
1
-
-
-
-
-
3
1
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1
-
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-
1
-
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-
1
1
-
1
-
-
-
-
1
-
-
2
1
-
-
-
1
-
-
-
-
3
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
740387
Yamashita
Direct electron transfer type ...
Burkholderia cepacia
Enzyme Microb. Technol.
52
123-128
2013
-
-
1
-
38
-
-
-
-
-
-
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3
-
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1
-
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2
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1
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1
1
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38
-
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1
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2
-
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-
-
-
-
723928
Zafar
Characterization of different ...
Aspergillus sp., Colletotrichum gloeosporioides, Komagataella pastoris
Anal. Bioanal. Chem.
402
2069-2077
2012
-
3
1
-
3
-
-
-
-
-
4
3
-
6
-
3
-
-
-
1
3
1
8
1
-
-
-
-
-
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