Any feedback?
Information on EC 3.1.1.20 - tannase and Organism(s) Aspergillus oryzae and UniProt Accession P78581
for references in articles please use BRENDA:EC3.1.1.20Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.1.1.20 tannaseIUBMB Comments
Also hydrolyses ester links in other tannins.
Specify your search results
Word Map
- 3.1.1.20
-
gallic
-
tannic
- aspergillus
- niger
- gallate
- plantarum
-
submerged
-
solid-state
- food industry
- catechin
- pectinase
- biotechnology
-
tannery
- gallotannins
-
galloylated
-
hydrolysable
-
paecilomyces
-
feruloyl
-
tannin-rich
- 1-propanol
-
depside
- emblica
- pentosus
- synthesis
- variotii
- degradation
- industry
- medicine
- agriculture
- brewing
- nutrition
The taxonomic range for the selected organisms is: Aspergillus oryzae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
tannase, fungal tannase, tannin acyl hydrolase, tanlpl, atan1, tansg1, aotanb, depsidase, tan410, lp-tan, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
tannin acylhydrolase
Also hydrolyses ester links in other tannins.
CAS REGISTRY NUMBER
COMMENTARY
9025-71-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(-)-catechin gallate + H2O
(-)-catechin + gallic acid
high activity
-
-
?
(-)-epicatechin gallate + H2O
(-)-epicatechin + gallic acid
best substrate
-
-
?
(-)-epigallocatechin gallate + H2O
(-)-epigallocatechin + gallic acid
moderate activity
-
-
?
methyl gallate + H2O
methanol + gallic acid
moderate activity
-
-
?
(-)-epicatechin gallate + H2O
(-)-epicatechin + gallic acid
-
-
-
?
(-)-epigallocatechin gallate + H2O
(-)-epigallocatechin + gallic acid
-
-
-
?
(-)-gallocatechin gallate + H2O
(-)-gallocatechin + gallic acid
-
-
-
?
1,2,3,4,6-pentagalloyl glucose + H2O
gallic acid + D-glucose
-
89% activity compared to methyl gallate
-
-
?
ethyl gallate + H2O
gallic acid + ethanol
-
55% activity compared to methyl gallate
-
-
?
ethyl protocatechuate + H2O
ethanol + protocatechuate
very low activity
-
-
?
isoamyl gallate + H2O
gallic acid + isoamyl alcohol
-
35% activity compared to methyl gallate
-
-
?
monogalloyl glucose + H2O
gallic acid + D-glucose
-
37% activity compared to methyl gallate
-
-
?
n-propyl gallate + H2O
gallic acid + n-propanol
-
55% activity compared to methyl gallate
-
-
?
tannic acid + H2O
10 gallate + D-glucose
-
the enzyme plays an important role in the complex tannin formation in plants and is involved in fruit ripening
-
?
tannic acid + H2O
gallic acid + ?
-
130% activity compared to methyl gallate
-
-
?
tannic acid + H2O
gallic acid + D-glucose
-
highest rate of tannase activity at 1.5-2.5% (w/v) tannic acid
-
-
?
additional information
?
-
tannase activity is assayed by monitoring the production of gallic acid, released from methyl gallate, through reaction with rhodanine. The enzyme has no activity with the methyl esters of ferulic, p-coumaric, caffeic, and sinapic acids, or with the ethyl, propyl, and butyl esters of 4-hydroxybenzoic acid. Substrate specificity, overview
-
-
?
additional information
?
-
-
tannase activity is assayed by monitoring the production of gallic acid, released from methyl gallate, through reaction with rhodanine. The enzyme has no activity with the methyl esters of ferulic, p-coumaric, caffeic, and sinapic acids, or with the ethyl, propyl, and butyl esters of 4-hydroxybenzoic acid. Substrate specificity, overview
-
-
?
additional information
?
-
tannase hydrolyzes different tannin-rich substrates. The highest relative activity is recorded for tannic acid (100%) followed by extract of china green tea (83.3%). Lower activity is obtained for the other tannin extracts of commercial red tea (42.3%), bark of Acacia nilotica (37.4%), leaves of Acacia nilotica (29.8%), bark of Acacia saligna (13.5%) and bark of Acacia ehrenbergina (4.2%). The high relative activity recorded for China green tea extract may be attributed to its richness with gallotannins mainly epigallocatechin gallate
-
-
?
additional information
?
-
-
tannase hydrolyzes different tannin-rich substrates. The highest relative activity is recorded for tannic acid (100%) followed by extract of china green tea (83.3%). Lower activity is obtained for the other tannin extracts of commercial red tea (42.3%), bark of Acacia nilotica (37.4%), leaves of Acacia nilotica (29.8%), bark of Acacia saligna (13.5%) and bark of Acacia ehrenbergina (4.2%). The high relative activity recorded for China green tea extract may be attributed to its richness with gallotannins mainly epigallocatechin gallate
-
-
?
additional information
?
-
-
no activities against the methyl esters of ferulic, 4-coumaric, caffeic, and sinapic acids, or the ethyl, propyl, and butyl esters of 4-hydroxybenzoic acid
-
-
?
additional information
?
-
the activity of recombinant AoTanB is lower toward natural substrates compared to that of AoTanA from Aspergillus oryzae
-
-
?
additional information
?
-
-
the activity of recombinant AoTanB is lower toward natural substrates compared to that of AoTanA from Aspergillus oryzae
-
-
?
additional information
?
-
recombinant enzyme AoTanB is able to release gallic acid from natural substrates, such as (-)-catechin gallate, (-)-epicatechin gallate, (-)-gallochatechin gallate, and (-)-epigallocatechin gallate. The enzyme also hydrolyzes ethyl protocatechuate. No activity is detected toward ethyl 4-hydroxybenzoate. The enzyme activity is determined via monitoring of the reaction between gallate and rhodanine
-
-
?
additional information
?
-
-
recombinant enzyme AoTanB is able to release gallic acid from natural substrates, such as (-)-catechin gallate, (-)-epicatechin gallate, (-)-gallochatechin gallate, and (-)-epigallocatechin gallate. The enzyme also hydrolyzes ethyl protocatechuate. No activity is detected toward ethyl 4-hydroxybenzoate. The enzyme activity is determined via monitoring of the reaction between gallate and rhodanine
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(-)-epicatechin gallate + H2O
(-)-epicatechin + gallic acid
-
-
-
?
(-)-epigallocatechin gallate + H2O
(-)-epigallocatechin + gallic acid
-
-
-
?
(-)-gallocatechin gallate + H2O
(-)-gallocatechin + gallic acid
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
-
the enzyme plays an important role in the complex tannin formation in plants and is involved in fruit ripening
-
?
additional information
?
-
the activity of recombinant AoTanB is lower toward natural substrates compared to that of AoTanA from Aspergillus oryzae
-
-
?
additional information
?
-
-
the activity of recombinant AoTanB is lower toward natural substrates compared to that of AoTanA from Aspergillus oryzae
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
FeSO4
-
at 5 mM, free enzyme: 61.3% inhibition, immobilized enzyme: 28% inhibition
HgCl2
-
5 mM, free enzyme: 13.7% inhibition, immobilized enzyme: 30% inhibition
Mg2+
Zn2+
additional information
Ca2+
-
CaCl2, 5 mM, no effect on the activity, both the free enzyme and the immoblized enzyme
Co2+
-
CoCl2 at 5 mM, free enzyme: 49.3% inhibition, immobilized enzyme: 24% inhibition
Cu2+
-
CuSO4 at 5 mM, free enzyme: 59% inhibition, immobilized enzyme: 44% inhibition
Mg2+
-
MgCl2 at 5 mM, free enzyme: 28.4% inhibition, immobilized enzyme: 14% inhibition
Zn2+
-
ZnCl2 at 5 mM, free enzyme: 55.4% inhibition, immobilized enzyme: 29.3% inhibition
additional information
-
no effect of the following metal ions at a concentration of 0.1 M: KCl, AlCl3, CdCl2 and SrCl2
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by benzoic acid and 3-methyl-benzoic acid
-
EDTA
-
activity is completely lost, when the enzyme is dialyzed against 0.025 M EDTA
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics and thermodynamics analysis, temperature dependence of kinetic parameters on tannic acid hydrolysis, overview
-
additional information
additional information
-
kinetics and thermodynamics analysis, temperature dependence of kinetic parameters on tannic acid hydrolysis, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
29.17
(-)-epigallocatechin gallate
recombinant enzyme, pH 6.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
5.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 8
-
immobilized enzyme, pH 3: 40% of the maximal activity, pH 8: 20% of the maximal activity. Free enzyme, pH 3: 5% of the maximal activity, pH 8: 20% of the maximal activity
4 - 5
-
tannase activity is greatly decreased below pH 4.0 and above pH 5.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 75
-
immobilized enzyme, 25°C: 40% of the maximal activity, 75°C: 18% of the maximal activity. Free enzyme, 25°C: 57% of the maximal activity, 75°C: 10% of the maximal activity
additional information
additional information
temperature dependence of kinetic parameters on tannic acid hydrolysis, overview
additional information
-
temperature dependence of kinetic parameters on tannic acid hydrolysis, overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
tannase catalyses the breakdown of ester and depside link-ages in hydrolysable tannins such as tannic acid, producing gallic acid and glucose
additional information
additional information
the catalytic triad residues of AoTanA are predicted to be Ser195, Asp455, and His501, with the serine and histidine residues brought together by a disulfide bond of the neighboring cysteines, Cys194 and Cys502. Functional role of the Kex2 recognition sites and disulfide bond between the neighboring cysteines in enzyme AoTanA, overview
additional information
-
the catalytic triad residues of AoTanA are predicted to be Ser195, Asp455, and His501, with the serine and histidine residues brought together by a disulfide bond of the neighboring cysteines, Cys194 and Cys502. Functional role of the Kex2 recognition sites and disulfide bond between the neighboring cysteines in enzyme AoTanA, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
1 * 33000 + 1 * 30000, purified tannase digested with N-glycosidase F and loaded with 2-mercaptoethanol, SDS-PAGE
33000
1 * 33000 + 1 * 30000, purified tannase digested with N-glycosidase F and loaded with 2-mercaptoethanol, SDS-PAGE
100000
-
x * 100000, SDS-PAGE, x * 31000 + x * 34000, SDS-PAGE after treatment with N-glycosidase F, x * 90000, mass spectrometry
290000
-
strain AO1, glycoprotein containing 22.7% sugars, a hetero-octamer with four pairs of two subunits, sedimentation equilibrium
30000
-
x * 30000 + x * 33000, four pairs of two subunits form a hetero-oligomer of a about 300000 Da native tannase, SDS-PAGE
31000
-
x * 100000, SDS-PAGE, x * 31000 + x * 34000, SDS-PAGE after treatment with N-glycosidase F, x * 90000, mass spectrometry
310000
-
strain AO1, glycoprotein containing 22.7% sugars, a hetero-octamer with four pairs of two subunits, gel filtration
33000
-
x * 30000 + x * 33000, four pairs of two subunits form a hetero-oligomer of a about 300000 Da native tannase, SDS-PAGE
34000
-
x * 100000, SDS-PAGE, x * 31000 + x * 34000, SDS-PAGE after treatment with N-glycosidase F, x * 90000, mass spectrometry
90000
-
x * 100000, SDS-PAGE, x * 31000 + x * 34000, SDS-PAGE after treatment with N-glycosidase F, x * 90000, mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
1 * 33000 + 1 * 30000, purified tannase digested with N-glycosidase F and loaded with 2-mercaptoethanol, SDS-PAGE
oligomer
-
x * 30000 + x * 33000, four pairs of two subunits form a hetero-oligomer of a about 300000 Da native tannase, SDS-PAGE
?
-
x * 100000, SDS-PAGE, x * 31000 + x * 34000, SDS-PAGE after treatment with N-glycosidase F, x * 90000, mass spectrometry
?
x * 90000-120000, glycosylated extracellular recombinant enzyme, SDS-PAGE, x * 65000, deglycosylated recombinant extracellular enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
the enzyme consists of two subunits that are generated by the cleavage of tannase gene product by the Kex2 protease, TanA has two Kex2 recognition sites at positions Arg311 and Arg316
glycoprotein
side-chain modification
-
glycoprotein, tannase I contains 5.4% and tannase II contains 5.4% neutral sugars, glucose-mannose-galactose, respectively
glycoprotein
recombinant enzyme expressed in Pichia pastoris, N-deglycosylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R311A/R316A
site-directed mutagenesis, the mutant exhibits the two bands similar to wild-type by SDS-PAGE after treatment with endoglycosidase H. The mutation has no effect on tannase activity and stability
additional information
additional information
construction of a seven amino-acid deletion variant of region Lys310eArg316 (mutant DELTAKR). The mutant shows only one band by SDS-PAGE after treatment with endoglycosidase H. The DELTAKR variant exhibits higher activity compared to the wild-type enzyme
additional information
-
construction of a seven amino-acid deletion variant of region Lys310eArg316 (mutant DELTAKR). The mutant shows only one band by SDS-PAGE after treatment with endoglycosidase H. The DELTAKR variant exhibits higher activity compared to the wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 8.5
purified native enzyme, 25°C, 180 min, over 50% activity remaining, completely stable at pH 4.5-7.0
750838
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 70
purified native enzyme, the calculated half-life times at 40, 45, 50, 55, 60, and 70°C are 955.15, 142.0, 30.28, 17.88, 8.23, and 2.95 min, respectively, determination of thermodynamic parameters for irreversible thermal inactivation at 40-70°C
40
purified extracellular recombinant enzyme, pH 6.0, 60 min, stable up to
40 - 50
-
the enzyme is stable up to 40°C. Native enzyme retains more than 70% of ist activity after incubation at 50°C for 60 min, whereas the residual activity of recombinant enzyme is approximately 40% after treatment at 50°C for 60 min
50
-
half-life of free enzyme: 90 min, half-life of immobilized enzyme: 120 min
60
-
half-life of free enzyme: 18 min, half-life of immobilized enzyme: 40 min
70
70
-
half-life of free enzyme: 8 min at, half-life of immobilized enzyme: 25 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
5°C, citrate buffer, pH 5.5 or distilled water, as purified powder or as a solution, maintains activity over 6 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native intracellular enzyme 36.7fold from submerged culture by ammonium sulfate fractionation, dialysis and desalting gel filtration, and two steps of gel filtration
recombinant wild-type and mutant enzymes from Pichia pastoris strain GS115 by anion exchange chromatography, ultrafiltration, and gel filtration
recombinant secreted enzyme from Pichia pastoris strain GS115 by anion exchange chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene tanA, recombinant expression of wild-type and mutant enzymes in Pichia pastoris strain GS115, recombinant AoTanA and its mutant variants are secreted using a Saccharomyces cerevisiae alpha-factor secretion signal peptide fusion, the recombinant proteins accumulate in the culture broth
cloned in Escherichia coli JM 109 and expressed in Aspergillus oryzae strain AO1, a tannase low-producing and nitrate reductase-deficient strain
-
gene AotanB, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, without the signal sequence, but with secretion signal sequence of Saccharomyces cerevisiae instead of the original signal sequence, recombinant expression in Pichia pastoris strain GS115 from vector pPICZalphaA, the enzyme is secreted into the medium. Recombinant AoTanB is highly expressed by incubation at 18°C compared to 30°C
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
addition of 0.05-0.5% (w/v) D-glucose favors the synthesis of tannase. NH4Cl is the most suitable nitrogen source for maximal tannase production. CaCl2 stimulates tannase production most efficiently. Tannic acid is the most favorable source of tannin for maximal tannase production
-
addition of D-glucose over 0.5% (w/v) concentration represses enzyme production. Addition of NaCl, MnSO4 or CdSO4 leads to decreased rate of tannase production
-
supplementation with maltose or glycerol inhibits tannase synthesis, which results in lower enzyme activity
-
tannic acid is an inducer. Supplementation with starch or sucrose increases enzyme production, but decreases the enzyme productivity. Maximum tannase activity (4.63 units/g of dry substrate) is obtained at 30°C, using 107 spores/g and 1.0% (w/v) sucrose as an additional carbon source. Yield of tannase increases as the inoculum size increases, with the maximal activity and productivity (3.50 units/g of dry substrate and 0.146 units/g of dry substrate/h, respectively) occurring when the cashew apple bagasse is inoculated with 107 spore/g and incubated for 24 h
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
biotechnology
-
synthesis of enzyme in fed-batch culture, at pH 5.0, achieves 7000 IU/l
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Iibuchi, S.; Minoda, Y.; Yamada, K.
Hydrolizing pathway, substrate specificity and inhibition of tannin acyl hydrolase of Asp. oryzae No. 7
Agric. Biol. Chem.
36
1553-1562
1972
Aspergillus oryzae, Aspergillus oryzae No. 7
-
Yamada, H.; Adachi, O.; Watanabe, M.; Sato, N.
Studies on fungal tannase. Part I. Formation, purification and catalytic properties of tannase of Aspergillus flavus
Agric. Biol. Chem.
32
1070-1078
1968
Aspergillus awamori, Aspergillus flavus, Aspergillus niger, Aspergillus oryzae, Aspergillus sojae, Aspergillus usamii, Aspergillus ustus, Penicillium chrysogenum, Penicillium expansum, Penicillium javanicum, Penicillium oxalicum
-
Iibuchi, S.; Minoda, Y.; Yamada, K.
Studies on tannin acyl hydrolase of microorganisms. Part III. Purification of the enzyme and some proporties of it
Agric. Biol. Chem.
32
803-809
1968
Aspergillus oryzae, Aspergillus oryzae No. 7
-
Abdel-Naby, M.A.; Sherif, A.A.; El-Tanash, A.B.; Mankarios, A.T.
Immobilization of Aspergillus oryzae tannase and properties of the immobilized enzyme
J. Appl. Microbiol.
87
108-114
1999
Aspergillus oryzae
-
Beverini, M.; Metche, M.
Identification, purification and physicochemical properties of tannase of Aspergillus orizae
Sci. Aliments
10
807-816
1990
Aspergillus oryzae
-
Hatamoto, O.; Watarai, T.; Kikuchi, M.; Mizusawa, K.; Sekine, H.
Cloning and sequencing of the gene encoding tannase and a structural study of the tannase subunit from Aspergillus oryzae
Gene
175
215-221
1996
Aspergillus oryzae
Aguilar, C.N.; Gutierrez-Sanchez, G.
Review: sources, properties, applications and potential uses of tannin acyl hydrolase
Food Sci. Technol. Int.
7
373-382
2001
Aspergillus fischeri, Aspergillus flavus, Aspergillus japonicus, Aspergillus niger, Aspergillus oryzae, Bos taurus, Cryphonectria parasitica, Fusarium solani, Phaseolus vulgaris, Rhizopus arrhizus, Trichoderma viride
-
Zhong, X.; Peng, L.; Zheng, S.; Sun, Z.; Ren, Y.; Dong, M.; Xu, A.
Secretion, purification, and characterization of a recombinant Aspergillus oryzae tannase in Pichia pastoris
Protein Expr. Purif.
36
165-169
2004
Aspergillus oryzae
Yu, X.; Li, Y.
Expression of Aspergillus oryzae tannase in Pichia pastoris and its application in the synthesis of propyl gallate in organic solvent
Food Technol. Biotechnol.
46
80-85
2008
Aspergillus oryzae (P78581)
-
Rodrigues, T.; Pinto, G.; Goncalves, L.
Effects of inoculum concentration, temperature, and carbon sources on tannase production during solid state fermentation of cashew apple bagasse
Biotechnol. Bioprocess Eng.
13
571-576
2008
Aspergillus oryzae
-
Abdel-Nabey, M.; Sherief, A.; EL-Tanash, A.
Tannin biodegradation and some factors affecting tannase production by two Aspergillus sp.
Biotechnology
10
149-158
2011
Aspergillus japonicus, Aspergillus oryzae
-
Mizuno, T.; Shiono, Y.; Koseki, T.
Biochemical characterization of Aspergillus oryzae native tannase and the recombinant enzyme expressed in Pichia pastoris
J. Biosci. Bioeng.
118
392-395
2014
Aspergillus oryzae, Aspergillus oryzae RIB 40
Koseki, T.; Otsuka, M.; Mizuno, T.; Shiono, Y.
Mutational analysis of Kex2 recognition sites and a disulfide bond in tannase from Aspergillus oryzae
Biochem. Biophys. Res. Commun.
482
1165-1169
2017
Aspergillus oryzae (P78581), Aspergillus oryzae, Aspergillus oryzae RIB 40 (P78581), Aspergillus oryzae ATCC 42149 (P78581)
Abdel-Naby, M.A.; El-Tanash, A.B.; Sherief, A.D.
Structural characterization, catalytic, kinetic and thermodynamic properties of Aspergillus oryzae tannase
Int. J. Biol. Macromol.
92
803-811
2016
Aspergillus oryzae (P78581), Aspergillus oryzae, Aspergillus oryzae RIB 40 (P78581), Aspergillus oryzae ATCC 42149 (P78581)
Koseki, T.; Ichikawa, K.; Sasaki, K.; Shiono, Y.
Characterization of a novel Aspergillus oryzae tannase expressed in Pichia pastoris
J. Biosci. Bioeng.
126
553-558
2018
Aspergillus oryzae (Q2UII1), Aspergillus oryzae, Aspergillus oryzae RIB 40 (Q2UII1), Aspergillus oryzae ATCC 42149 (Q2UII1)
EXTERNAL LINKS (specific for EC-Number 3.1.1.20)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
