Information on EC 3.1.1.20 - tannase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.1.1.20
-
RECOMMENDED NAME
GeneOntology No.
tannase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
digallate + H2O = 2 gallate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
hydrolysis of carboxylic ester
Penicillium variabile
-
-
hydrolysis of carboxylic ester
-
-
hydrolysis of carboxylic ester
-
-
hydrolysis of carboxylic ester
-
-
hydrolysis of carboxylic ester
-
-
hydrolysis of carboxylic ester
-
-
hydrolysis of carboxylic ester
-
the enzyme also shows beta-glucosidase activity
hydrolysis of carboxylic ester
-
-
hydrolysis of carboxylic ester
-
-
hydrolysis of carboxylic ester
Aspergillus aculeatus DBF 9, Aspergillus niger MTCC 2425, Bacillus licheniformis KBR 6
-
-
-
SYSTEMATIC NAME
IUBMB Comments
tannin acylhydrolase
Also hydrolyses ester links in other tannins.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
depsidase
Caesalpinia coriaria
-
-
fungal tannase
-
-
fungal tannase
Aspergillus niger Aa-20
-
-
-
gallotannin-degrading esterase
Caesalpinia coriaria
-
-
plant tannase
Caesalpinia coriaria
-
-
Tan410
E7D7J5
-
tannase
Aspergillus awamori MTCC9299
-
-
-
tannase
Aspergillus niger GH1
-
-
-
tannase
Aspergillus tamarii IMI388810 (B)
-
-
-
tannase
Bacillus licheniformis KBR6
-
-
-
tannase
Hyalopus sp.
-
-
tannase
Hyalopus sp. DSF3
-
-
-
tannase
Lactobacillus plantarum CECT 748T
-
-
-
tannase I
-
degrades ester-containing polygallol derivatives
tannase II
-
hydrolzes polygallol derivatives containing depside groups
tannin acyl hydrolase
-
-
tannin acyl hydrolase
Aspergillus aculeatus DBF 9
-
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
C7F6Y1
-
tannin acyl hydrolase
Aspergillus awamori BTMFW032
-, C7F6Y1
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
Aspergillus foetidus MTCC 6322
-
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
Aspergillus heteromorphus MTCC 8818
-
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
Aspergillus niger GH1, Aspergillus niger MTCC 2425
-
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
Aspergillus oryzae No. 7
-
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
Bacillus licheniformis KBR 6, Bacillus licheniformis KBR6
-
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
C7EDT0
-
tannin acyl hydrolase
Enterobacter sp. KPJ103
C7EDT0
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
B3Y018
tannase
tannin acyl hydrolase
Lactobacillus plantarum CECT 748T
-
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
Penicillium variabile
-
belongs to the class of serine hydrolases
tannin acyl hydrolase
Penicillium variabile IARI 2031
-
belongs to the class of serine hydrolases
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
Rhizopus sp.
-
-
tannin acyl hydrolase
Rhizopus sp. C3-I
-
-
-
tannin acyl hydrolase
-
-
tannin acyl hydrolase
Trichoderma sp.
-
-
tannin acyl hydrolase
E7D7J5
-
tannin acyl hydrolase
-
-
tannin acyl-hydrolase
-
-
tannin acyl-hydrolase
Corynebacterium sp. Q40
-
-
-
tannin acyl-hydrolase
-
-
tannin acyl-hydrolase
Klebsiella pneumoniae Q52
-
-
-
tannin acyl-hydrolase
-
-
tannin acyl-hydrolase
Paenibacillus polymyxa Q47
-
-
-
tannin acylhydrolase
B3Y018
-
tannin acylhydrolase
-
-
tannin-acyl-hydrolase
-
-
tannin-acyl-hydrolase
Bacillus licheniformis KBR6
-
-
-
yeast tannase
Candida sp.
-
-
yeast tannase
Candida sp. K-1
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9025-71-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain DBF 9, intra-and extracellular enzyme forms, inducible, fungus can utilize tannic acid as sole carbon and energy source
-
-
Manually annotated by BRENDA team
strain DBF9
-
-
Manually annotated by BRENDA team
Aspergillus aculeatus DBF 9
strain DBF 9, intra-and extracellular enzyme forms, inducible, fungus can utilize tannic acid as sole carbon and energy source
-
-
Manually annotated by BRENDA team
Aspergillus aculeatus DBF9
strain DBF9
-
-
Manually annotated by BRENDA team
var. Nakazawa
-
-
Manually annotated by BRENDA team
Aspergillus awamori BTMFW032
-
-
-
Manually annotated by BRENDA team
Aspergillus awamori BTMFW032
-
UniProt
Manually annotated by BRENDA team
Aspergillus awamori MTCC9299
MTCC9299
-
-
Manually annotated by BRENDA team
IFO 5839
-
-
Manually annotated by BRENDA team
isolated from a composite tannery effluent collected from a local tannery
-
-
Manually annotated by BRENDA team
GMRB013 MTCC 3557
-
-
Manually annotated by BRENDA team
strain GMRB 013 MTCC 3557
-
-
Manually annotated by BRENDA team
strain MTCC 6322
-
-
Manually annotated by BRENDA team
Aspergillus foetidus GMRB 013 MTCC 3557
strain GMRB 013 MTCC 3557
-
-
Manually annotated by BRENDA team
Aspergillus foetidus MTCC 6322
strain MTCC 6322
-
-
Manually annotated by BRENDA team
Aspergillus heteromorphus MTCC 8818
-
-
-
Manually annotated by BRENDA team
inducible enzyme
-
-
Manually annotated by BRENDA team
IRDUAM collection strain No. Aa20
-
-
Manually annotated by BRENDA team
PKL 104
-
-
Manually annotated by BRENDA team
strain Aa-20
-
-
Manually annotated by BRENDA team
strain ATCC 16620
-
-
Manually annotated by BRENDA team
strain GH1
-
-
Manually annotated by BRENDA team
strain HA37
-
-
Manually annotated by BRENDA team
strain MTCC 2425
-
-
Manually annotated by BRENDA team
strain MTCC 2425, and a strain isolated from a composite tannery effluent collected from a local tannery
-
-
Manually annotated by BRENDA team
strain van Tieghem MTCC 2425
-
-
Manually annotated by BRENDA team
Aspergillus niger Aa-20
strain Aa-20
-
-
Manually annotated by BRENDA team
Aspergillus niger GH1
-
-
-
Manually annotated by BRENDA team
Aspergillus niger GH1
strain GH1
-
-
Manually annotated by BRENDA team
Aspergillus niger HA37
strain HA37
-
-
Manually annotated by BRENDA team
Aspergillus niger LCF 8
LCF 8
-
-
Manually annotated by BRENDA team
Aspergillus niger MTCC 2425
strain MTCC 2425
-
-
Manually annotated by BRENDA team
Aspergillus niger PKL 104
PKL 104
-
-
Manually annotated by BRENDA team
2 isozymes
-
-
Manually annotated by BRENDA team
expression in Pichia pastoris
-
-
Manually annotated by BRENDA team
Aspergillus oryzae No. 7
No. 7
-
-
Manually annotated by BRENDA team
strain SHL 6, induction of enzyme by growth on peptone
-
-
Manually annotated by BRENDA team
Aspergillus sp. SHL 6
strain SHL 6, induction of enzyme by growth on peptone
-
-
Manually annotated by BRENDA team
IMI388810 (B)
-
-
Manually annotated by BRENDA team
Aspergillus tamarii IMI388810 (B)
IMI388810 (B)
-
-
Manually annotated by BRENDA team
strain DBS66, isolated from forest soil in india
-
-
Manually annotated by BRENDA team
Aureobasidium pullulans DBS66
strain DBS66, isolated from forest soil in india
-
-
Manually annotated by BRENDA team
KBR 9, inducible enzyme
-
-
Manually annotated by BRENDA team
strain KBR 6
-
-
Manually annotated by BRENDA team
strain KBR 6 isolated from lateritic soil, inducible enzyme
-
-
Manually annotated by BRENDA team
strain KBR6
-
-
Manually annotated by BRENDA team
strain KBR6, inducible enzyme
-
-
Manually annotated by BRENDA team
Bacillus licheniformis KBR 6
strain KBR 6
-
-
Manually annotated by BRENDA team
Bacillus licheniformis KBR 6
strain KBR 6 isolated from lateritic soil, inducible enzyme
-
-
Manually annotated by BRENDA team
Bacillus licheniformis KBR6
strain KBR6
-
-
Manually annotated by BRENDA team
Bacillus licheniformis KBR6
strain KBR6, inducible enzyme
-
-
Manually annotated by BRENDA team
synonym Blastobotrys adeninivorans
-
-
Manually annotated by BRENDA team
Blastobotrys adeninivorans LS3
strain LS3
Uniprot
Manually annotated by BRENDA team
Caesalpinia coriaria
i.e. Divi-Divi
-
-
Manually annotated by BRENDA team
Candida sp.
-
-
-
Manually annotated by BRENDA team
Candida sp.
K-1
-
-
Manually annotated by BRENDA team
Candida sp. K-1
K-1
-
-
Manually annotated by BRENDA team
Corynebacterium sp. Q40
Q40
-
-
Manually annotated by BRENDA team
synonym Aspergillus nidulans
-
-
Manually annotated by BRENDA team
Enterobacter sp. KPJ103
-
UniProt
Manually annotated by BRENDA team
isolated from a composite tannery effluent collected from a local tannery
-
-
Manually annotated by BRENDA team
Hyalopus sp.
strain DSF3
-
-
Manually annotated by BRENDA team
Hyalopus sp. DSF3
strain DSF3
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae Q52
Q52
-
-
Manually annotated by BRENDA team
CECT 748T strain
-
-
Manually annotated by BRENDA team
inducible enzyme
-
-
Manually annotated by BRENDA team
strain ATCC 14917(T)
SwissProt
Manually annotated by BRENDA team
strain CECT 748(T), ATCC 14917, DSMZ 20174
-
-
Manually annotated by BRENDA team
Lactobacillus plantarum CECT 748(T)
strain CECT 748(T), ATCC 14917, DSMZ 20174
-
-
Manually annotated by BRENDA team
Lactobacillus plantarum CECT 748T
-
-
-
Manually annotated by BRENDA team
Lactobacillus plantarum CECT 748T
CECT 748T strain
-
-
Manually annotated by BRENDA team
strain ASR-S1, induction of enzyme by solid-state fermentation on tamarind seed powder, wheat bran, or coffee husk
-
-
Manually annotated by BRENDA team
Lactobacillus sp. ASR-S1
strain ASR-S1, induction of enzyme by solid-state fermentation on tamarind seed powder, wheat bran, or coffee husk
-
-
Manually annotated by BRENDA team
a strain isolated in Sao Paulo, Brazil
-
-
Manually annotated by BRENDA team
Paenibacillus polymyxa Q47
Q47
-
-
Manually annotated by BRENDA team
Penicillium chrysogenum NCIM-722
NCIM-722
-
-
Manually annotated by BRENDA team
isolated from a composite tannery effluent collected from a local tannery
-
-
Manually annotated by BRENDA team
Penicillium variabile
-
-
-
Manually annotated by BRENDA team
Penicillium variabile
strain IARI 2031
-
-
Manually annotated by BRENDA team
Penicillium variabile IARI 2031
strain IARI 2031
-
-
Manually annotated by BRENDA team
Qercus pedunculata
-
-
Manually annotated by BRENDA team
RO IIT RB-13, NRRL 21498
-
-
Manually annotated by BRENDA team
strain RO IIT RB-13, NRRL 21498
-
-
Manually annotated by BRENDA team
Rhizopus oryzae RO IIT RB-13
strain RO IIT RB-13, NRRL 21498
-
-
Manually annotated by BRENDA team
Rhizopus sp.
strain C3-I
-
-
Manually annotated by BRENDA team
Rhizopus sp. C3-I
strain C3-I
-
-
Manually annotated by BRENDA team
subsp. ruminantium
-
-
Manually annotated by BRENDA team
Trichoderma sp.
isolated from a composite tannery effluent collected from a local tannery
-
-
Manually annotated by BRENDA team
Antarctic strain P9, two cold-adapted isozymes TAH I and TAH II
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
the enzyme production follows logarithmic growth phase with maximum enzyme yield being obtained after 6 days corresponding to the culture pH of 3.8
physiological function
-
tanA gene is specific to Staphylococcus lugdunensis
physiological function
B7VFD0, -
enzyme titre with the recombinant strain (390 U/l) is approximately 10times higher than that in the control strain without the TEF1 promoter-ATAN1 gene expression cassette. The Atan1 protein contains at positions 210-214 the canonical Gly-X-Ser-X-Gly motif found in the serine hydrolases as the catalytic triad for nucleophilic serine
physiological function
C7EDT0
tannase and the organism itself are employed to protect grazing animals and environment against the toxic effects caused by tannins in them
physiological function
Aspergillus tamarii IMI388810 (B)
-
the enzyme production follows logarithmic growth phase with maximum enzyme yield being obtained after 6 days corresponding to the culture pH of 3.8
-
physiological function
Enterobacter sp. KPJ103
-
tannase and the organism itself are employed to protect grazing animals and environment against the toxic effects caused by tannins in them
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+/-)-epicatechin-gallate + H2O
epicatechin + gallate
show the reaction diagram
-
-
-
-
?
(+/-)-epigallocatechin-3-gallate + H2O
epigallocatechin + gallate
show the reaction diagram
-
-
-
-
?
(-)-epicatechin gallate + H2O
(-)-epicatechin + gallic acid
show the reaction diagram
-
from green tea leaves
-
-
?
(-)-epigallocatechin gallate + H2O
(-)-epigallocatechin + gallic acid
show the reaction diagram
-
from green tea leaves
-
-
?
1,2,3,4,6-pentagalloyl glucose + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
-
1,2,3,4,6-pentagalloyl glucose + H2O
gallic acid + D-glucose
show the reaction diagram
-
89% activity compared to methyl gallate
-
-
?
1,2,3,6-tetra-O-galloyl-beta-D-glucose + H2O
?
show the reaction diagram
-
-
-
-
?
1,2,6-tri-O-galloyl-beta-D-glucose + H2O
?
show the reaction diagram
-
-
-
-
?
1,6-di-O-galloyl-beta-D-glucose + H2O
?
show the reaction diagram
-
-
-
-
?
1-O-anisoyl-beta-D-glucose + H2O
anisic acid + glucose
show the reaction diagram
-
-
-
-
?
1-O-benzoyl-beta-D-glucose + H2O
benzoic acid + beta-D-glucose
show the reaction diagram
-
-
-
-
?
1-O-galloyl-beta-D-glucose + H2O
gallic acid + beta-D-glucose
show the reaction diagram
-
-
-
-
-
1-O-galloyl-beta-D-glucose + H2O
gallic acid + beta-D-glucose
show the reaction diagram
-
-
-
-
?
1-O-p-hydroxybenzoyl-beta-D-glucose + H2O
4-hydroxybenzoate + beta-D-glucose
show the reaction diagram
-
-
-
-
?
1-O-protocatechuoyl-beta-D-glucose + H2O
protocatechuate + glucose
show the reaction diagram
-
-
-
-
?
1-O-syringoyl-beta-D-glucose + H2O
4-hydroxy-3,5-dimethoxy benzoic acid + beta-D-glucose
show the reaction diagram
-
-
-
-
?
1-O-vanilloyl-beta-D-glucose + H2O
4-hydroxy-3-methoxy benzoic acid + beta-D-glucose
show the reaction diagram
-
-
-
-
?
1-O-veratroyl-beta-D-glucose + H2O
3,4-dimethyoxy benzoic acid + beta-D-glucose
show the reaction diagram
-
-
-
-
?
1-propanol + gallic acid
propyl gallate + H2O
show the reaction diagram
-
the reaction takes place in organic solvents, best in benzene, effect of water content, overview
-
-
r
3,6-di-O-galloyl-beta-D-glucose + H2O
?
show the reaction diagram
-
-
-
-
?
4-O-digalloyl-1,2,3,6-tetra-O-galloyl-beta-D-glucose + H2O
?
show the reaction diagram
-
-
-
-
?
6-O-galloyl-beta-D-glucose + H2O
gallic acid + beta-D-glucose
show the reaction diagram
-
-
-
-
?
catechin gallate + H2O
gallic acid + catechin
show the reaction diagram
-
-
-
?
catechin gallate + H2O
gallic acid + catechin
show the reaction diagram
B7VFD0, -
best substrate
-
-
?
cellobiose + H2O
D-glucose
show the reaction diagram
-
beta-glucosidase activity of the enzyme, only observed in absence of tannic acid
-
?
chlorogenic acid + H2O
?
show the reaction diagram
-
-
-
-
?
chlorogenic acid + H2O
trans-caffeate + quinate
show the reaction diagram
E7D7J5
complete hydrolysis within 40 min
-
-
?
digallate + H2O
gallate
show the reaction diagram
-
-
-
?
digallate + H2O
gallate
show the reaction diagram
-
-
-
?
digallate + H2O
gallate
show the reaction diagram
-
-
-
?
digallate + H2O
gallate
show the reaction diagram
-
-
-
?
digallate + H2O
gallate
show the reaction diagram
B3Y018, -
-
-
-
?
digallate + H2O
gallate
show the reaction diagram
-
substrate: tannins
-
?
digallate + H2O
gallate
show the reaction diagram
-
substrate: tannins
i.e. 3,4,5-trihydroxybenzoate
?
digallate + H2O
gallate
show the reaction diagram
-
substrate: tannins
i.e. 3,4,5-trihydroxybenzoate
?
digallate + H2O
gallate
show the reaction diagram
Aspergillus aculeatus DBF 9
-
substrate: tannins
-, i.e. 3,4,5-trihydroxybenzoate
?
digallate + H2O
gallate
show the reaction diagram
Bacillus licheniformis KBR 6
-
substrate: tannins
i.e. 3,4,5-trihydroxybenzoate
?
ellagitannin + H2O
hexahydroxydiphenic acid + ?
show the reaction diagram
-
-
-
-
?
ellagitannins + H2O
hexahydroxydiphenic acid + gallic acid
show the reaction diagram
Aspergillus niger, Caesalpinia coriaria, Aspergillus niger Aa-20
-
-
-
-
?
epicatechin gallate + H2O
gallic acid + epicatechin
show the reaction diagram
-
-
-
?
epicatechin gallate + H2O
gallic acid + epicatechin
show the reaction diagram
-
-
-
-
?
epicatechin gallate + H2O
gallic acid + epicatechin
show the reaction diagram
B7VFD0, -
-
-
-
?
epicatechin gallate + H2O
gallate + epicatechin
show the reaction diagram
E7D7J5
complete hydrolysis within 40 min
-
-
?
epigallocatechin gallate + H2O
gallic acid + epigallocatechin
show the reaction diagram
-
-
-
-
?
epigallocatechin gallate + H2O
gallic acid + epigallocatechin
show the reaction diagram
-
-
-
?
epigallocatechin gallate + H2O
gallic acid + epigallocatechin
show the reaction diagram
-
-
-
-
?
epigallocatechin gallate + H2O
gallic acid + epigallocatechin
show the reaction diagram
-
-
-
-
?
epigallocatechin gallate + H2O
gallic acid + epigallocatechin
show the reaction diagram
B7VFD0, -
-
-
-
?
epigallocatechin gallate + H2O
gallic acid + epigallocatechin
show the reaction diagram
Lactobacillus plantarum CECT 748T
-
-
-
-
?
epigallocatechin gallate + H2O
gallate + epigallocatechin
show the reaction diagram
E7D7J5
complete hydrolysis within 40 min
-
-
?
ethyl ferulate + H2O
ethanol + ferulate
show the reaction diagram
E7D7J5
complete hydrolysis within 40 min
-
-
?
ethyl gallate + H2O
gallic acid + ethanol
show the reaction diagram
-
-
-
-
?
ethyl gallate + H2O
gallic acid + ethanol
show the reaction diagram
-
-
-
-
?
ethyl gallate + H2O
gallic acid + ethanol
show the reaction diagram
Aspergillus oryzae, Aspergillus oryzae No. 7
-
55% activity compared to methyl gallate
-
-
?
ethyl gallate + H2O
gallic acid + ethanol
show the reaction diagram
Lactobacillus plantarum CECT 748T
-
-
-
-
?
gallate + 1-butanol
1-butyl gallate + H2O
show the reaction diagram
-
85% of the yield with 1-propanol
-
-
r
gallate + 1-hexanol
1-hexyl gallate + H2O
show the reaction diagram
-
2% of the yield with 1-propanol
-
-
r
gallate + 1-pentanol
1-pentyl gallate + H2O
show the reaction diagram
-
77% of the yield with 1-propanol
-
-
r
gallate + ethanol
ethyl gallate + H2O
show the reaction diagram
-
5% of the yield with 1-propanol
-
-
r
gallate + methanol
methyl gallate + H2O
show the reaction diagram
-
2% of the yield with 1-propanol
-
-
r
gallate + propan-1-ol
propyl gallate + H2O
show the reaction diagram
-
-
-
-
r
gallic acid ethyl ester + H2O
gallic acid + ethanol
show the reaction diagram
B7VFD0, -
-
-
-
?
gallic acid methyl ester + H2O
gallic acid + methanol
show the reaction diagram
-
-
-
?
gallic acid propyl ester + H2O
gallic acid + propanol
show the reaction diagram
B7VFD0, -
-
-
-
?
gallocatechin gallate + H2O
gallic acid + gallocatechin
show the reaction diagram
-
-
-
-
?
gallocatechin gallate + H2O
gallic acid + gallocatechin
show the reaction diagram
B7VFD0, -
-
-
-
?
gallocatechin gallate + H2O
gallic acid + gallocatechin
show the reaction diagram
-
best substrate
-
?
gallocatechin gallate + H2O
gallic acid + gallocatechin
show the reaction diagram
Lactobacillus plantarum CECT 748T
-
-
-
-
?
gallotannin + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
gallotannin + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
gallotannin + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
gallotannin + H2O
gallic acid + D-glucose
show the reaction diagram
Rhizopus sp.
-
-
-
-
?
gallotannin + H2O
gallic acid + D-glucose
show the reaction diagram
Caesalpinia coriaria
-
-
-
-
?
gallotannin + H2O
gallic acid + D-glucose
show the reaction diagram
-
hydrolysis of ester and depside linkages of gallotannins via galloylglucose
-
-
?
gallotannin + H2O
gallic acid + D-glucose
show the reaction diagram
Aspergillus niger Aa-20
-
-, hydrolysis of ester and depside linkages of gallotannins via galloylglucose
-
-
?
gallotannin + H2O
gallic acid + D-glucose
show the reaction diagram
Bacillus licheniformis KBR 6
-
-, hydrolysis of ester and depside linkages of gallotannins via galloylglucose
-
-
?
gallotannin + H2O
gallic acid + D-glucose
show the reaction diagram
Rhizopus sp. C3-I
-
-
-
-
?
isoamyl gallate + H2O
gallic acid + isoamyl alcohol
show the reaction diagram
-
35% activity compared to methyl gallate
-
-
?
lauryl gallate + H2O
gallic acid + lauric acid
show the reaction diagram
-
-
-
-
?
m-digallate + H2O
gallate
show the reaction diagram
-
-
-
-
?
meta-digallic acid + H2O
gallic acid
show the reaction diagram
-
-
-
-
?
meta-digallic acid + H2O
gallic acid
show the reaction diagram
-
-
-
-
?
methyl 3,4,5-trihydroxybenzoate + H2O
methanol + 3,4,5-trihydroxybenzoate
show the reaction diagram
Aspergillus niger, Aspergillus niger GH1
-
-
-
-
?
methyl gallate + 1-propanol
propyl gallate + ?
show the reaction diagram
Lactobacillus plantarum, Lactobacillus plantarum CECT 748T
-
transesterification, synthetic yields of 45% are obtained with 30% of 1-propanol at pH 5.0
-
-
?
methyl gallate + H2O
gallic acid + methanol
show the reaction diagram
-
-
-
?
methyl gallate + H2O
gallic acid + methanol
show the reaction diagram
-
-
-
-
?
methyl gallate + H2O
gallic acid + methanol
show the reaction diagram
-
-
-
?
methyl gallate + H2O
gallic acid + methanol
show the reaction diagram
-
-
-
-
?
methyl gallate + H2O
gallic acid + methanol
show the reaction diagram
-
-
-
?
methyl gallate + H2O
gallic acid + methanol
show the reaction diagram
-
-
-
-
?
methyl gallate + H2O
gallic acid + methanol
show the reaction diagram
-
-
-
?
methyl gallate + H2O
gallic acid + methanol
show the reaction diagram
-
-
-
-
?
methyl gallate + H2O
gallic acid + methanol
show the reaction diagram
-
-
-
-
?
methyl gallate + H2O
gallic acid + methanol
show the reaction diagram
Penicillium variabile
-
-
-
-
?
methyl gallate + H2O
gallic acid + methanol
show the reaction diagram
B3Y018, -
-
-
-
?
methyl gallate + H2O
gallic acid + methanol
show the reaction diagram
Aspergillus oryzae No. 7
-
-
-
-
?
methyl gallate + H2O
gallic acid + methanol
show the reaction diagram
Penicillium variabile IARI 2031
-
-
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
-
-
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
-
-
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
-
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
-
-
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
-
-
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
B7VFD0, -
-
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
-
-
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
-
-
-
-
r
methyl gallate + H2O
gallate + methanol
show the reaction diagram
C7EDT0
-
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
C7F6Y1
best substrate
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
-
recombinant tannase shows similar affinity for both methyl gallate and ethyl gallate
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
Aspergillus niger GH1
-
-
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
Lactobacillus plantarum CECT 748(T)
-
-
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
Aspergillus awamori BTMFW032
C7F6Y1
best substrate
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
Lactobacillus plantarum CECT 748T
-
-
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
Lactobacillus plantarum CECT 748T
-
recombinant tannase shows similar affinity for both methyl gallate and ethyl gallate
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
Enterobacter sp. KPJ103
C7EDT0
-
-
-
?
methyl gallate + H2O
gallate + methanol
show the reaction diagram
Aspergillus niger MTCC 2425
-
-
-
?
methyl gallate + H2O
methanol + gallate
show the reaction diagram
-
-
-
-
?
n-propyl gallate + H2O
gallic acid + n-propanol
show the reaction diagram
-
-
-
-
?
n-propyl gallate + H2O
gallic acid + n-propanol
show the reaction diagram
Penicillium variabile
-
-
-
-
?
n-propyl gallate + H2O
gallic acid + n-propanol
show the reaction diagram
Aspergillus oryzae, Aspergillus oryzae No. 7
-
55% activity compared to methyl gallate
-
-
?
n-propyl gallate + H2O
gallic acid + n-propanol
show the reaction diagram
Penicillium variabile IARI 2031
-
-
-
-
?
propyl gallate + H2O
gallate + propanol
show the reaction diagram
-
-
-
-
?
propyl gallate + H2O
gallate + propanol
show the reaction diagram
-
-
-
?
propyl gallate + H2O
gallate + propanol
show the reaction diagram
P78581
-
-
-
r
propyl gallate + H2O
gallate + propanol
show the reaction diagram
C7F6Y1
-
-
-
?
propyl gallate + H2O
gallate + propanol
show the reaction diagram
E7D7J5
46% hydrolysis within 40 min
-
-
?
propyl gallate + H2O
gallate + propanol
show the reaction diagram
Aspergillus awamori BTMFW032
C7F6Y1
-
-
-
?
propyl gallate + H2O
gallate + propanol
show the reaction diagram
Aspergillus niger MTCC 2425
-
-
-
?
propyl gallate + H2O
propanol + gallate
show the reaction diagram
-
-
-
-
?
propyl gallate + H2O
gallic acid + propanol
show the reaction diagram
-
-
-
-
?
propyl gallate + H2O
gallate + 1-propanol
show the reaction diagram
Lactobacillus plantarum, Lactobacillus plantarum CECT 748T
-
-
-
-
?
protocatechuic acid ethyl ester + H2O
protocatechuate + ethanol
show the reaction diagram
-
-
-
-
?
pyrogallol + H2O
?
show the reaction diagram
-
-
-
-
?
rhodanine + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
rosmarinic acid + H2O
(2E)-3,4-dihydroxycinnamate + (2R)-3-(3,4-dihydroxyphenyl)-2-hydroxypropanoate
show the reaction diagram
E7D7J5
88% hydrolysis within 40 min
-
-
?
tannic acid + 1-propanol
propyl gallate + ?
show the reaction diagram
Lactobacillus plantarum, Lactobacillus plantarum CECT 748T
-
transesterification, synthetic yields of 45% are obtained with 30% of 1-propanol at pH 5.0
-
-
?
tannic acid + 10 H2O
10 gallic acid + glucose
show the reaction diagram
-
-
-
?
tannic acid + 10 H2O
10 gallic acid + glucose
show the reaction diagram
-
-
-
?
tannic acid + 10 H2O
10 gallic acid + glucose
show the reaction diagram
-
-
-
?
tannic acid + 10 H2O
10 gallic acid + glucose
show the reaction diagram
Penicillium variabile
-
gallotannin from fruits of Terminalia chebula
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
Candida sp.
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
Aspergillus oryzae, Aspergillus oryzae No. 7
-
130% activity compared to methyl gallate
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
Aspergillus oryzae No. 7
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
Klebsiella pneumoniae Q52
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
Aspergillus niger PKL 104
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
Penicillium chrysogenum NCIM-722
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
Aspergillus niger LCF 8
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
Candida sp. K-1
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
Paenibacillus polymyxa Q47
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
Aspergillus aculeatus DBF9
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
Aureobasidium pullulans DBS66
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
Corynebacterium sp. Q40
-
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
Candida sp.
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
specific for
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
best substrate
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
enzyme hydrolyzes the ester and depside linkages of tannic acid
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
the enzyme plays an important role in the complex tannin formation in plants and is involved in fruit ripening
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
Aspergillus aculeatus DBF 9
-
enzyme hydrolyzes the ester and depside linkages of tannic acid
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
Aspergillus oryzae No. 7
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
Klebsiella pneumoniae Q52
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
Bacillus licheniformis KBR 6
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
Paenibacillus polymyxa Q47
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
Aspergillus niger MTCC 2425
-
best substrate
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
Corynebacterium sp. Q40
-
-
-
?
tannic acid + H2O
?
show the reaction diagram
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
Candida sp.
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
Aspergillus oryzae No. 7
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
Klebsiella pneumoniae Q52
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
Aspergillus niger PKL 104
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
Penicillium chrysogenum NCIM-722
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
Aspergillus niger LCF 8
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
Candida sp. K-1
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
Paenibacillus polymyxa Q47, Corynebacterium sp. Q40
-
-
-
-
-
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
Fusarium sp., Trichoderma sp.
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
Penicillium variabile
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
Penicillium variabile
-
tannins from Chebulina myrobalan
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
Lactobacillus plantarum CECT 748(T)
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
Bacillus licheniformis KBR 6
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
Rhizopus oryzae RO IIT RB-13, Aspergillus foetidus GMRB 013 MTCC 3557
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
Penicillium variabile IARI 2031
-
-, tannins from Chebulina myrobalan
-
-
?
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
Penicillium variabile
-
best substrate
-
-
?
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
-
from green tea leaves
-
-
?
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
E7D7J5
complete hydrolysis within 40 min
-
-
?
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
Aspergillus niger GH1
-
-
-
-
?
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
Aspergillus foetidus MTCC 6322
-
-
-
-
?
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
Penicillium variabile IARI 2031
-
best substrate
-
-
?
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
Bacillus licheniformis KBR6
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
B7VFD0, -
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
Hyalopus sp.
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
C7EDT0
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
C7F6Y1
lowest activity
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
at least 95% of tannic acid is transformed into pure gallate
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
highest rate of tannase activity at 1.5-2.5% (w/v) tannic acid
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
Aspergillus heteromorphus MTCC 8818
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
Aspergillus tamarii IMI388810 (B)
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
Aspergillus niger GH1
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
Hyalopus sp. DSF3
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
Aspergillus awamori MTCC9299
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
Aspergillus awamori BTMFW032
C7F6Y1
lowest activity
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
Enterobacter sp. KPJ103
C7EDT0
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
Bacillus licheniformis KBR6
-
-
-
-
?
tannic acid + n-propanol
propyl gallate
show the reaction diagram
Aspergillus awamori, Aspergillus awamori BTMFW032
-
transesterification, 3.2% conversion
-
-
?
tannin + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannin + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannin + H2O
gallate + D-glucose
show the reaction diagram
-
tannin is degraded by 55% while a combination of tannin and gelatin (1:1) results in 60% of tannin degradation
-
-
?
monogalloyl glucose + H2O
gallic acid + D-glucose
show the reaction diagram
-
37% activity compared to methyl gallate
-
-
?
additional information
?
-
-
the enzyme removes gallic acid non-specifically from both condensed and hydrolysable tannins
-
?
additional information
?
-
-
production of phytate in beans
-
?
additional information
?
-
-
the enzyme hydrolyzes the ester and depside bonds of gallotannins and gallic acid esters
-
?
additional information
?
-
-
tannase-treated green tea leaf extract shows increased inhibition activity on N-nitrosamine formation of secondary amines due to increased catechin levels compared to untreated leaf extract, the inhibitory effect is also higher as with ascorbic acid, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the degradation of condensed tannins, complex tannins, gallotannins, and ellagitannins produced by different plant species in almost all tissue types, e.g. bark, wood, leaf, fruit, root and seed, overview, tannin structure and physiologic effects, degradation mechanism, and pathways, detailed overview
-
-
-
additional information
?
-
Q0KKP0, -
the tannase from Staphylococcus lugdunensis is associated with colon cancer in the human host, comparison of isolation of tannase-producing bacteria between colon cancer, adenoma, and normal groups, overview
-
-
-
additional information
?
-
-
tannase catalyzes the hydrolysis of ester and depside bonds in hydrolysable tannins or gallic acid esters liberating glucose or gallic acid
-
-
-
additional information
?
-
-
tannase cleaves ester bonds between gallic acid and glucose in tannic acid and m-digallic acid ester linkages, named depside bonds, it also hydrolyzes (+)-epicatechin gallate and (+)-epigallocatechin-3-gallate
-
-
-
additional information
?
-
-
the enzyme catalyses the hydrolysis of ester and depside bonds in hydrolysable tannin such as tannic acid, releasing glucose and gallic acid
-
-
-
additional information
?
-
-
almost no activity with starch, D-glucose, D-sucrose, and D-xylan
-
-
-
additional information
?
-
-
tannases hydrolyze only those substrates that contain at least two phenolic OH groups in the acid component. The esterified COOH group must be on the oxidized benzene ring and must not be ortho to one of the OH groups. Benzoic esters (methyl benzoate, and ethyl benzoate), hydroxybenzoic esters (methyl 4-hydroxybenzoate, ethyl 4-hydroxybenzoate, propyl 4-hydroxybenzoate, and butyl 4-hydroxybenzoate), vanillic ester (methyl vanillate), gentisic ester (methyl gentisate), salicylic ester (methyl salicylate), ferulic esters (ferulic methyl ester and ferulic ethyl ester), ellagic, chlorogenic acids, quercetin, catechin, epicatechin, gallocatechin, epigallocatechin or 4-nitrophenyl beta-D-glucopyranoside are not metabolized
-
-
-
additional information
?
-
Aspergillus niger Aa-20, Bacillus licheniformis KBR 6
-
the enzyme is involved in the degradation of condensed tannins, complex tannins, gallotannins, and ellagitannins produced by different plant species in almost all tissue types, e.g. bark, wood, leaf, fruit, root and seed, overview, tannin structure and physiologic effects, degradation mechanism, and pathways, detailed overview
-
-
-
additional information
?
-
Lactobacillus plantarum CECT 748T
-
tannases hydrolyze only those substrates that contain at least two phenolic OH groups in the acid component. The esterified COOH group must be on the oxidized benzene ring and must not be ortho to one of the OH groups. Benzoic esters (methyl benzoate, and ethyl benzoate), hydroxybenzoic esters (methyl 4-hydroxybenzoate, ethyl 4-hydroxybenzoate, propyl 4-hydroxybenzoate, and butyl 4-hydroxybenzoate), vanillic ester (methyl vanillate), gentisic ester (methyl gentisate), salicylic ester (methyl salicylate), ferulic esters (ferulic methyl ester and ferulic ethyl ester), ellagic, chlorogenic acids, quercetin, catechin, epicatechin, gallocatechin, epigallocatechin or 4-nitrophenyl beta-D-glucopyranoside are not metabolized
-
-
-
additional information
?
-
Bacillus licheniformis KBR6
-
the enzyme catalyses the hydrolysis of ester and depside bonds in hydrolysable tannin such as tannic acid, releasing glucose and gallic acid
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
digallate + H2O
gallate
show the reaction diagram
-
substrate: tannins
i.e. 3,4,5-trihydroxybenzoate
?
digallate + H2O
gallate
show the reaction diagram
Aspergillus aculeatus, Aspergillus aculeatus DBF 9
-
substrate: tannins
i.e. 3,4,5-trihydroxybenzoate
?
digallate + H2O
gallate
show the reaction diagram
Bacillus licheniformis KBR 6
-
substrate: tannins
i.e. 3,4,5-trihydroxybenzoate
?
ellagitannin + H2O
hexahydroxydiphenic acid + ?
show the reaction diagram
-
-
-
-
?
ellagitannins + H2O
hexahydroxydiphenic acid + gallic acid
show the reaction diagram
Aspergillus niger, Caesalpinia coriaria, Aspergillus niger Aa-20
-
-
-
-
?
gallotannin + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + 10 H2O
10 gallic acid + glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
enzyme hydrolyzes the ester and depside linkages of tannic acid
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
-
the enzyme plays an important role in the complex tannin formation in plants and is involved in fruit ripening
-
?
tannic acid + H2O
?
show the reaction diagram
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
Candida sp.
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
-
-
-
-
-
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
Fusarium sp., Trichoderma sp.
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
Penicillium variabile
-
-
-
-
?
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
C7EDT0
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
-
at least 95% of tannic acid is transformed into pure gallate
-
-
?
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
Aspergillus aculeatus DBF 9
-
enzyme hydrolyzes the ester and depside linkages of tannic acid
-
?
tannic acid + H2O
?
show the reaction diagram
Aspergillus oryzae No. 7
-
-
-
-
-
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
Aspergillus niger GH1
-
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
Lactobacillus plantarum CECT 748(T)
-
-
-
-
?
tannic acid + H2O
?
show the reaction diagram
Klebsiella pneumoniae Q52
-
-
-
-
-
tannic acid + H2O
10 gallate + D-glucose
show the reaction diagram
Bacillus licheniformis KBR 6
-
-
-
?
tannic acid + H2O
gallate + ?
show the reaction diagram
Bacillus licheniformis KBR 6
-
-
-
-
?
tannic acid + H2O
?
show the reaction diagram
Aspergillus niger PKL 104
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
Penicillium chrysogenum NCIM-722
-
-
-
-
-
tannic acid + H2O
gallate + ?
show the reaction diagram
Rhizopus oryzae RO IIT RB-13
-
-
-
-
?
tannic acid + H2O
?
show the reaction diagram
Aspergillus niger LCF 8
-
-
-
-
-
tannic acid + H2O
?
show the reaction diagram
Candida sp. K-1
-
-
-
-
-
tannic acid + H2O
gallate + ?
show the reaction diagram
Aspergillus foetidus GMRB 013 MTCC 3557
-
-
-
-
?
tannic acid + H2O
?
show the reaction diagram
Paenibacillus polymyxa Q47
-
-
-
-
-
tannic acid + H2O
gallate + ?
show the reaction diagram
Penicillium variabile IARI 2031
-
-
-
-
?
tannic acid + H2O
gallic acid + D-glucose
show the reaction diagram
Enterobacter sp. KPJ103
C7EDT0
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
Aspergillus aculeatus DBF9
-
-
-
-
?
tannic acid + H2O
gallic acid + ?
show the reaction diagram
Aureobasidium pullulans DBS66
-
-
-
-
?
tannic acid + H2O
gallate + D-glucose
show the reaction diagram
Bacillus licheniformis KBR6
-
-
-
-
?
tannic acid + H2O
?
show the reaction diagram
Corynebacterium sp. Q40
-
-
-
-
-
tannin + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
tannin + H2O
gallate + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
production of phytate in beans
-
?
additional information
?
-
-
the enzyme hydrolyzes the ester and depside bonds of gallotannins and gallic acid esters
-
?
additional information
?
-
-
tannase-treated green tea leaf extract shows increased inhibition activity on N-nitrosamine formation of secondary amines due to increased catechin levels compared to untreated leaf extract, the inhibitory effect is also higher as with ascorbic acid, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the degradation of condensed tannins, complex tannins, gallotannins, and ellagitannins produced by different plant species in almost all tissue types, e.g. bark, wood, leaf, fruit, root and seed, overview, tannin structure and physiologic effects, degradation mechanism, and pathways, detailed overview
-
-
-
additional information
?
-
Q0KKP0, -
the tannase from Staphylococcus lugdunensis is associated with colon cancer in the human host, comparison of isolation of tannase-producing bacteria between colon cancer, adenoma, and normal groups, overview
-
-
-
additional information
?
-
Aspergillus niger Aa-20, Bacillus licheniformis KBR 6
-
the enzyme is involved in the degradation of condensed tannins, complex tannins, gallotannins, and ellagitannins produced by different plant species in almost all tissue types, e.g. bark, wood, leaf, fruit, root and seed, overview, tannin structure and physiologic effects, degradation mechanism, and pathways, detailed overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(NH4)6Mo7O24
-
0.1 M, no effect on activity
Ba2+
-
117.94% activity at 1 mM
BaCl2
-
0.1 M, no effect on activity
Br-
-
activates both isozymes TAH I and TAH II
Ca2+
-
highly stable in presence of 1 mM CaCl2
Ca2+
-
at 1 mM stimulates by 16%
Ca2+
-
1 mM increases activity by 81%
Ca2+
-
105.6% activity at 1 mM
Ca2+
E7D7J5
126% activity at 1 mM
Ca2+
-
109.51% activity at 1 mM
Ca2+
-
Ca(CH3COO)2: 33% inhibition, at 20 mM concentration
Ca2+
Candida sp.
-
Ca(CH3COO)2: no effect at a concentration of 45 mM at 30C
Ca2+
-
CaCl2: 0.1 M, no effect on activity
Ca2+
-
CaCl2, 5 mM, no effect on the activity, both the free enzyme and the immoblized enzyme
Ca2+
-
CaCl2, no effect on the activity
Cd2+
E7D7J5
121% activity at 1 mM
Co2+
-
133.59% activity at 1 mM
Co2+
-
Co(NO3)2: 36% inhibition, at 20 mM concentration
Co2+
Candida sp.
-
CoCl2: no effect at a concentration of 45 mM at 30C
Co2+
-
0.1 M, no effect on activity
Co2+
-
CoCl2 at 5 mM, free enzyme: 49.3% inhibition, immobilized enzyme: 24% inhibition
Co2+
-
CoCl2 no effect on activity
Cu+
-
108.6% activity at 1 mM
Cu2+
-
highly stable in presence of 1 mM CuSO4
Cu2+
-
106.2% activity at 1 mM
Cu2+
E7D7J5
108% activity at 1 mM
Cu2+
-
108.44% activity at 1 mM
Cu2+
-
CuSO4: 53% inhibition, at 20 mM concentration
Cu2+
Candida sp.
-
CuSO4: no effect at a concentration of 45 mM at 30C
Cu2+
-
CuCl2: 70% inhibition, 0.1 M
Cu2+
-
CuSO4 at 5 mM, free enzyme: 59% inhibition, immobilized enzyme: 44% inhibition
Cu2+
-
CuSO4: 68% inhibition
Fe2+
-
107.6% activity at 1 mM
Fe3+
C7F6Y1
144.44% activity at 10 mM
FeCl3
-
0.1 M, no effect on activity
FeCl3
-
13% inhibition
FeSO4
-
45% inhibition, at 20 mM concentration
FeSO4
-
at 5 mM, free enzyme: 61.3% inhibition, immobilized enzyme: 28% inhibition
Hg2+
-
137.73% activity at 1 mM
HgCl2
-
5 mM, free enzyme: 13.7% inhibition, immobilized enzyme: 30% inhibition
K+
-
at 1 mM stimulates by 9%
K+
-
1 mM increases activity by 26%
K+
C7F6Y1
176.62% activity at 10 mM
K+
-
115.18% activity at 1 mM
Mg2+
-
activates both isozymes TAH I and TAH II
Mg2+
-
activates
Mg2+
-
at 1 mM stimulates by 23.9%
Mg2+
E7D7J5
120% activity at 1 mM
Mg2+
-
118.25% activity at 1 mM
Mg2+
-
MgSO4: 17% inhibition, at 20 mM concentration
Mg2+
Candida sp.
-
MgCl2, MgSO4: no effect at a concentration of 45 mM at 30C
Mg2+
-
MgCl2: no effect on activity
Mg2+
-
MgCl2 at 5 mM, free enzyme: 28.4% inhibition, immobilized enzyme: 14% inhibition
Mg2+
-
MgSO4 no effect on activity
Mn2+
-
highly stable in presence of 1 mM MnSO4
Mn2+
-
at 1 mM stimulates by 15.23%
Mn2+
-
115.8% activity at 1 mM
Mn2+
-
MnSO4: 22% inhibition, at 20 mM concentration
Mn2+
-
0.1 M, no effect on activity
Na+
-
highly stable in presence of 1 mM NaCl
Na+
-
at 1 mM stimulates by 11%
Na+
C7F6Y1
120.37% activity at 20 mM
Na+
-
124.69% activity at 1 mM
NH4Cl
-
110.74% activity at 1 mM
Ni2+
-
NiCl2: 42% inhibition, at 20 mM concentration
Ni2+
Candida sp.
-
NiSO4, no effect at a concentration of 45 mM at 30C
Ni2+
-
NiSO4: 0.1 M, no effect on activity
Urea
-
activates both isozymes TAH I and TAH II
Zn2+
-
142% activity at 1 mM
Zn2+
-
ZnCl2: 22% inhibition, ZnSO4: 45% inhibition, at 20 mM concentration
Zn2+
Candida sp.
-
no effect of ZnCl2 and ZnSO4 at a concentration of 45 mM at 30C
Zn2+
-
ZnCl2 70% inhibition, 0.1 M
Zn2+
-
ZnCl2 at 5 mM, free enzyme: 55.4% inhibition, immobilized enzyme: 29.3% inhibition
Zn2+
-
ZnCl2 39% inhibition
Mn2+
-
MnCl2 no effect on activity
additional information
-
-
additional information
-
no effect at 1 mM by K+, Ca2+, Zn2+, and urea
additional information
-
1 mM EDTA has no significant effect
additional information
-
Ba2+ has no significant effect on tannase activity up to 3 mM
additional information
E7D7J5
the enzyme is not influenced by Zn2+ and Co2+
additional information
-
no effect of the following metal ions at a concentration of 0.1 M: KCl, AlCl3, CdCl2 and SrCl2
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
slight inhibition, 1 mM, 88% remaining activity
1,10-phenanthroline
Penicillium variabile
-
-
1,10-phenanthroline
Penicillium variabile
-
40% residual activity at 1 mM
1,10-phenanthroline
-
42% inhibition at 1 mM
1,2,3-trihydroxybenzoic acid
-
competitive; i.e. pyrogallol
-
1,2-dihydroxybenzene
-
competitive
1,3-dihydroxybenzene
-
competitive
1,4-dihydroxybenzene
-
competitive
1-Propanol
-
activates at a concentration of 3.6-7.3% v/v, at higher concentration it inhibits the propyl gallate synthesis reaction causing disruption of essential membrane functions and denaturation of enzyme
1-Propanol
-
inhibits the enzymatic hydrolysis of propyl gallate
2,3-Dihydroxybenzoic acid
-
competitive
2,5-dihydroxybenzoic acid
-
competitive
2,6-dihydroxybenzoic acid
-
noncompetitive
2-hydroxybenzoic acid
-
competitive
2-mercaptoethanol
-
1 mM, 68.3% remaining activity
2-mercaptoethanol
-
inhibits both isozymes TAH I and TAH II
2-mercaptoethanol
-
41% inhibition at 1 mM
2-mercaptoethanol
-
39% inhibition at 1 mM
3,4-dihydroxybenzoic acid
-
competitive
3,5-Dihydroxybenzoic acid
-
competitive
3-Hydroxybenzoic acid
-
competitive
4-Aminobenzoic acid
-
25% inhibition at 1 mM
4-Aminobenzoic acid
-
81.9% residual activity at 1 mM
4-chloromercuribenzoate
-
inhibits both isozymes TAH I and TAH II
4-hydroxybenzoic acid
-
competitive
8-hydroxyquinoline
Penicillium variabile
-
47.2% residual activity at 1 mM
acetic acid
-
completely inhibits activity
acetone
Penicillium variabile
-
complete inactivation
acetone
-
gradual decrease in activity with increasing concentration, at 60%, activity is reduced to 55.01%
acetone
-
at 60% of concentration, completely inhibits activity at 30C
Ag+
-
slight competitive inhibition at 1 mM, 82.4% remaining activity
Ag+
-
inhibits both isozymes TAH I and TAH II
Ag+
-
57% residual activity at 5 mM
Ag+
E7D7J5
51% residual activity at 1 mM
AgNO3
-
98.77% residual activity at 1 mM
Al3+
E7D7J5
97% residual activity at 1 mM
Al3+
C7F6Y1
complete inhibition at 1 mM
Al3+
-
75.14% residual activity at 1 mM
alpha-glutathione
-
inhibits both isozymes TAH I and TAH II
Ba2+
-
competitive inhibition at 1 mM, 5.4% remaining activity
Ba2+
-
competitive inhibitor
Ba2+
C7F6Y1
complete inhibition at 5 mM
Benzene
-
98% residual activity at 5% (v/v)
Benzoic acid
-
83.1% residual activity at 1 mM
beta-mercaptoethanol
Penicillium variabile
-
-
beta-mercaptoethanol
-
1 mM inhibits activity by 85%
beta-mercaptoethanol
-
59.4% residual activity at 1 mM
beta-mercaptoethanol
E7D7J5
63% residual activity at 1 mM
beta-mercaptoethanol
C7F6Y1
-
beta-mercaptoethanol
-
37.07% residual activity at 20 mM
Bromoacetic acid
Penicillium variabile
-
-
Bromoacetic acid
Penicillium variabile
-
53.3% residual activity at 1 mM
Ca2+
-
58% inhibition at 20 mM, noncompetitive
Ca2+
-
slight competitive inhibition at 1 mM, 86.6% remaining activity
Ca2+
-
7% inhibition of tannase produced under submerged fermentation at 1 mM
Ca2+
C7F6Y1
0.84% residual activity at 20 mM
CaCl2
-
noncompetitive
carbon tetrachloride
Penicillium variabile
-
complete inactivation
Cd2+
-
55% inhibition at 20 mM, noncompetitive
Cd2+
-
inhibits both isozymes TAH I and TAH II
Cd2+
B7VFD0, -
45% inhibition, at 30C in sodium citrate buffer, pH 6.0
Cd2+
-
57% residual activity at 5 mM
Cd2+
C7F6Y1
11.82% residual activity at 20 mM
Chloroform
-
completely inhibits activity
Co2+
-
complete inhibition at 1 mM
Co2+
-
inhibits both isozymes TAH I and TAH II
Co2+
-
at 1 mM inhibits by 71.14%
Co2+
-
competitive inhibitor
Co2+
-
87.6% residual activity at 1 mM
Co2+
C7F6Y1
39.06% residual activity at 20 mM
CO32-
-
inhibits both isozymes TAH I and TAH II
Cr2+
E7D7J5
52% residual activity at 1 mM
Cu2+
-
inhibits both isozymes TAH I and TAH II
Cu2+
-
at 1 mM inhibits by 51.21%
Cu2+
-
ca. 20% inhibition after 60 min of incubation at 30C and pH 5
Cu2+
-
competitive inhibitor
Cu2+
B7VFD0, -
51% inhibition, at 30C in sodium citrate buffer, pH 6.0
Cu2+
-
41% inhibition of tannase produced under solid-state fermentation at 1 mM
Cu2+
C7F6Y1
10.58% residual activity at 20 mM
cyanamide
Penicillium variabile
-
-
cyanamide
Penicillium variabile
-
61.7% residual activity at 1 mM
cysteine
-
38% inhibition at 1 mM
D-glucose
-
slightly stimulating, inhibits intracellular enzyme production at concentrations above 0.05% w/v, and extracellular enzyme production above 0.1% w/v
diisopropylfluorophosphate
-
DFP, inhibition is not immediate, but requires a period of preincubation of the enzyme. 1 mol of 32P of DFP is incorporated into 1 mol of enzyme to give complete inhibition, suggest that the enzyme contains one essential serine per mol enzyme, a typical serine enzyme
diisopropylfluorophosphate
-
83% inhibition
dithiothreitol
Penicillium variabile
-
54.1% residual activity at 1 mM
dithiothreitol
C7F6Y1
displays inhibitory properties at higher concentrations of 1.0% to 5.0% (v/v)
DMSO
-
1 mM, 19% remaining activity
DTT
Penicillium variabile
-
-
EDTA
-
1 mM, 30% remaining activity
EDTA
-
complete inhibition at 5 mM
EDTA
-
38% inhibition at 1 mM
EDTA
-
at 0.01% of concentration 22% inhibition after 5 min and at 0.1% of concentration 19% inhibition after 60 min at 30C
EDTA
-
35% inhibition at 1 mM
EDTA
E7D7J5
86% residual activity at 1 mM
EDTA
-
25.89% residual activity at 20 mM
EDTA
Candida sp.
-
95% remaining activity after 3 days at a concentration of 10 mM, pH 7.2, 0.1 M phosphate buffer
EDTA
-
activity is completely lost, when the enzyme is dialyzed against 0.025 M EDTA
ethanol
Penicillium variabile
-
-
ethanol
-
inhibits by 48.84% initially, thereafter complete loss in the enzyme activity at 40% and 60%
ethanol
-
at 60% of concentration, completely inhibits activity at 30C
ethanol
-
80.2% residual activity at 5% (v/v)
ethyl gallate
-
20% inhibition at 1 mM
ethyl gallate
-
1 mM inhibits activity by 48%
Fe2+
-
63% inhibition of tannase produced under submerged fermentation at 1 mM
-
Fe3+
-
complete inhibition at 1 mM
-
Fe3+
-
inhibits both isozymes TAH I and TAH II
-
Fe3+
-
at 1 mM inhibits by 76.89%
-
Fe3+
-
more than 40% inhibition after 5 min and 60 min of incubation at 30C and pH 5
-
Fe3+
-
competitive inhibitor
-
Fe3+
B7VFD0, -
35% inhibition, at 30C in sodium citrate buffer, pH 6.0
-
Fe3+
-
85.74% residual activity at 1 mM
-
formaldehyde
Penicillium variabile
-
complete inactivation
formaldehyde
-
51.5% inhibition at 20% after 60 min at 30C
gallate
-
inhibits the enzymatic hydrolysis of propyl gallate
Gallic acid
-
activates at a concentration up to 0.005 mM, at higher concentration it inhibits the propyl gallate synthesis reaction
Gallic acid
B7VFD0, -
competitive inhibition using gallic acid as substrate
Gallic acid
-
82.1% residual activity at 1 mM
Gallic acid
-
competitive; i.e. 3,4,5-trihydroxybenzoic acid
H2O2
C7F6Y1
H2O2 concentrations of less than 2% and higher than 10% lead to a decline in enzyme activity
heptane
Penicillium variabile
-
-
heptane
-
at 60% of concentration 95% inhibition after 60 min at 30C
Hg2+
-
competitive inhibition at 1 mM, 13.8% remaining activity
Hg2+
-
inhibits both isozymes TAH I and TAH II
Hg2+
-
66% inhibition at 1 mM
Hg2+
-
1 mM inhibits activity by 78%
Hg2+
-
56% residual activity at 5 mM
Hg2+
E7D7J5
complete inhibition at 1 mM
Hg2+
C7F6Y1
53.02% residual activity at 20 mM
iodoacetic acid
Penicillium variabile
-
-
iodoacetic acid
Penicillium variabile
-
48% residual activity at 1 mM
Isoamylalcohol
-
completely inhibits activity
Isopropanol
-
96.3% residual activity at 5% (v/v)
Isopropyl alcohol
-
completely inhibits activity
K+
-
inhibits both isozymes TAH I and TAH II
K+
-
73.3% residual activity at 5 mM
Li+
C7F6Y1
3.07% residual activity at 20 mM
mercuribenzoic acid
Penicillium variabile
-
48.8% residual activity at 1 mM
mercuric benzoic acid
Penicillium variabile
-
-
-
methanol
-
initial inhibitory effect at 20% and 40%, original activity is regained at 60%
methanol
-
95.8% residual activity at 5% (v/v)
Mg2+
-
33% inhibition at 20 mM, noncompetitive
Mg2+
-
16% inhibition at 1 mM
Mg2+
-
slight reduction in activity in the presence of Mg2+
Mg2+
-
1 mM inhibits activity by 12%
Mg2+
-
ca. 20% inhibition after 5 min of incubation at 30C and pH 5
Mg2+
-
77.5% residual activity at 5 mM
Mg2+
C7F6Y1
7.03% residual activity at 20 mM
Mn2+
-
54% inhibition at 20 mM, noncompetitive
Mn2+
-
inhibits both isozymes TAH I and TAH II
Mn2+
-
ca. 20% inhibition after 5 min of incubation at 30C and pH 5
Mn2+
-
79% residual activity at 1 mM
Mn2+
E7D7J5
90% residual activity at 1 mM
Mn2+
C7F6Y1
10.18% residual activity at 20 mM
N-bromosuccinic acid
-
73.9% residual activity at 1 mM
-
N-bromosuccinimide
-
29% inhibition at 1 mM
N-ethylmaleimide
Penicillium variabile
-
7% residual activity at 1 mM
Na+
-
89.1% residual activity at 5 mM
NaCl
-
inhibits above 3 M
NaCl
E7D7J5
the enzyme retains 80% activity at 5 M
NEM
Penicillium variabile
-
81% inhibition
Pb2+
-
inhibits both isozymes TAH I and TAH II
petroleum ether
Penicillium variabile
-
-
-
phenyl boronic acid
Penicillium variabile
-
-
phenyl boronic acid
Penicillium variabile
-
67.1% residual activity at 1 mM
phenyl methyl sulphonyl fluoride
B7VFD0, -
95% inhibition, at 30C in sodium citrate buffer, pH 6.0
phenylmethylsulfonyl fluoride
Penicillium variabile
-
28% residual activity at 1 mM
phenylmethylsulfonyl fluoride
-
38% inhibition after 5 min of incubation at 30C and pH 5, indicating the presence of a serine or cysteine residue in the catalytic site
phenylmethylsulfonyl fluoride
-
86.1% residual activity at 1 mM
phenylmethylsulfonyl fluoride
E7D7J5
32% residual activity at 1 mM
PMSF
Penicillium variabile
-
72% inhibition
propranolol hydrochloride
Penicillium variabile
-
-
propranolol hydrochloride
Penicillium variabile
-
49.6% residual activity at 1 mM
propyl gallate
-
85.1% residual activity at 1 mM
pyrogallol
-
95% residual activity at 1 mM
SDS
Penicillium variabile
-
complete inactivation
SDS
-
at 0.01% of concentration 15% inhibition after 60 min at 30C
Sn2+
-
inhibits both isozymes TAH I and TAH II
Sodium azide
-
36% inhibition at 1 mM
Sodium azide
-
82.8% residual activity at 1 mM
Sodium bisulfite
-
25% inhibition at 1 mM
Sodium bisulfite
-
81.3% residual activity at 1 mM
Sodium cholate
Penicillium variabile
-
-
Sodium cholate
Penicillium variabile
-
52.6% residual activity at 1 mM
sodium dodecyl sulphate
-
inhibits isozyme TAH II
sodium lauryl sulfate
-
-
sodium lauryl sulfate
-
above 2%
Sodium thioglycolate
-
83.1% residual activity at 1 mM
soybean extract
-
inhibits at 0.05-1.0% w/v
-
tetrahydrofuran
Penicillium variabile
-
complete inactivation
tetrahydrofuran
-
at 60% of concentration, completely inhibits activity at 30C
Toluene
Penicillium variabile
-
-
Toluene
-
gradual decrease in activity with increasing concentration, at 60%, activity is reduced to 28.49%
Triton X 100
-
1 mM inhibits activity by 20%
Triton X-100
-
inhibits both isozymes TAH I and TAH II
Triton X-100
-
48% inhibition at 1% v/v
Triton X-100
-
32% inhibition at 1 mM
Triton X-100
-
21.9% inhibition at 1% (v/v)
Tween
-
1 mM inhibits activity by 20%
Tween 20
-
inhibits both isozymes TAH I and TAH II
Tween 20
-
30% inhibition at 1% v/v
Tween 20
-
30.8% inhibition at 1% (v/v)
Tween 40
-
activation up to 0.05% v/v, complete inhibition at 0.6% v/v; activation up to 0.4% v/v, complete inhibition at 0.6% v/v
Tween 60
-
complete inhibition at 1% v/v
Tween 60
-
inhibits both isozymes TAH I and TAH II
Tween 80
-
inhibits both isozymes TAH I and TAH II
Tween 80
-
30% inhibition at 1% v/v
Tween 80
-
at 0.01% of concentration 35% inhibition after 5 min at 30C
Tween 80
-
27.4% inhibition at 1% (v/v)
Tween 80
E7D7J5
47% residual activity at 1 mM
Tween-60
Penicillium variabile
-
complete inactivation
Tween-80
Penicillium variabile
-
complete inactivation
Urea
-
at 1.5 M maximal enhancement of activity, at 3 M 50% inhibition
Urea
-
slightly activates the enzyme at 0.5 M, but inhibits at higher concentration, 50% inhibition at 3 M
Urea
-
1 mM inhibits activity by 52%
Zn2+
-
41% inhibition at 20 mM, noncompetitive
Zn2+
-
competitive inhibition at 1 mM, 21.3% remaining activity
Zn2+
-
inhibits both isozymes TAH I and TAH II
Zn2+
-
slight reduction in activity in the presence of Zn2+
Zn2+
-
1 mM inhibits activity by 18%
Zn2+
-
ca. 10% inhibition after 5 min and 60 min of incubation at 30C and pH 5
Zn2+
-
competitive inhibitor
Zn2+
-
80% residual activity at 5 mM
Zn2+
C7F6Y1
30.54% residual activity at 20 mM
Mo2+
C7F6Y1
22.48% residual activity at 20 mM
additional information
-
no inhibition of the extracellular enzyme by PMSF
-
additional information
-
not affected by EDTA
-
additional information
Penicillium variabile
-
no inhibition by Triton X-100
-
additional information
-
no inhibition at 1 mM iodoacetamide
-
additional information
-
-
-
additional information
-
no effect at 1 mM by K+, Ca2+, Zn2+, Tween 80, urea, DMSO, and EDTA
-
additional information
-
induction and repression patterns, overview
-
additional information
-
the enzyme is not affected by EDTA
-
additional information
-
1 mM Zn2+ has no effect
-
additional information
-
1 mM DMSO has no significant effect
-
additional information
-
at 0.1% and 0.01% of concentration, Ca2+, Tween 20 and Triton X-100 have no effect at 30C
-
additional information
B7VFD0, -
EDTA, Mg2+, Mn2+, Ca2+, Zn2+ and EDTA have no or only weak effects
-
additional information
-
not inhibited by iodoacetamide
-
additional information
E7D7J5
the enzyme is not inhibited by 1-4 M NaCl
-
additional information
-
not inhibited by benzoic acid and 3-methyl-benzoic acid
-
additional information
-
not inhibited by o-phenanthroline, PMSF, EDTA, 2-mercaptomethanol, sodium thioglycolate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-Propanol
-
activates at a concentration of 3.6-7.3% v/v, at higher concentration it inhibits the propyl gallate synthesis reaction causing disruption of essential membrane functions and denaturation of enzyme
ammonium chloride
-
0.1% w/v, 4fold increased activity when used as nitrogen source
ammonium nitrate
-
0.1% w/v, 1.2fold increased activity when used as nitrogen source
ammonium sulfate
-
with FeSO4, when used as nitrogen source, 1.7fold increase in activity
Benzene
-
optimum enzyme concentration should be 0.1 g mycelial dry weight per 10 ml benzene
Benzene
-
increases activity by 2fold at 60% v/v concentration
Br-
-
1.6fold induction
butanol
-
increases activity by 2fold at 60% v/v concentration
D-glucose
-
glucose has a stimulatory effect on tannase synthesis in vivo at 0.1% w/v concentration
dithiothreitol
C7F6Y1
enhances activity at low concentrations of 0.2% (v/v) (108.1% residual activity) to 0.6% (v/v) (111.8% residual activity)
Gallic acid
-
activates at a concentration up to 0.005 mM, at higher concentration it inhibits the propyl gallate synthesis reaction
heptane
-
at 20% of concentration increases activity by 19% after 60 min, and at 60% of concentration by 97% after 6 min
Hg+
-
slight activation at 1 mM, 105% activity
Mg2+
-
activation at 1 mM, 137.9% activity
N,N-Dimethylformamide
-
-
petroleum ether
-
at 20% of concentration increases activity by 19% after 60 min, and at 60% of concentration by 73% after 6 min
-
S2O32-
-
2.2fold induction
SDS
-
138.96% activity at 0.01% (v/v)
Sodium cholate
Penicillium variabile
-
-
sodium lauryl sulfate
-
45% increase of activity at 1% (v/v)
sodium taurocholate
Penicillium variabile
-
-
Sodium thioglycolate
C7F6Y1
an increase in residual enzyme activity from 23.1% (0.2% concentration) to a maximum of 321.2% (1.0% concentration) is noted along with an increase in its concentration
Tannic acid
-
required for enzyme induction, best at 1% w/v tannic acid for the intracellular enzyme, and at 2% w/v for the extracellular enzyme
Tannic acid
-
enzyme is inducible
Tannic acid
-
maximum enzyme production (9.38 U/ml) is recorded after 96 h of incubation at 35C, initial pH 5, in submerged culture (200 rpm) utilising 2% (w/v) tannic acid as a sole carbon source
Triton X-100
-
121.63% activity at 0.01% (v/v)
Tween 40
-
best at 0.4% v/v, above that concentration it inhibits the enzyme
Tween 80
-
best at 0.05% v/v, above that concentration it inhibits the enzyme
Tween 80
-
at 0.1% of concentration increases activity by 25% after 60 min
Urea
-
at 1.5 M maximal enhancement of activity, at 3 M 50% inhibition
Urea
-
slightly activates the enzyme at 0.5 M, but inhibits at higher concentration, 50% inhibition at 3 M
Urea
E7D7J5
106% activity at 1 mM
additional information
-
not affected by EDTA
-
additional information
-
no effect at 1 mM by Tween 80, DMSO, and EDTA
-
additional information
-
induction and repression patterns, overview
-
additional information
-
the enzyme is not affected by EDTA
-
additional information
-
poor activating effects by octane and dodecane, tannic acid induces the enzyme, effects of organic solvents on propyl gallate production by the enzyme, and effect of water content, overview
-
additional information
-
Tween 20 and Triton X-100 have no effect
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5.9
-
1,2,3,4,6-pentagalloyl glucose
-
-
6.9
-
1,2,3,6-tetra-O-galloyl-beta-D-glucose
-
-
2.3
-
1,2,6-Tri-O-galloyl-beta-D-glucose
-
-
1.3
-
1,6-di-O-galloyl-beta-D-glucose
-
-
12.7
-
1-O-anisoyl-beta-D-glucose
-
-
2
-
1-O-benzoyl-beta-D-glucose
-
-
0.14
-
1-O-Galloyl-beta-D-glucose
-
-
9.1
-
1-O-Galloyl-beta-D-glucose
-
-
2.1
-
1-O-p-hydroxybenzoyl-beta-D-glucose
-
-
6
-
1-O-Protocatechuoyl-beta-D-glucose
-
-
0.85
-
1-O-syringoyl-beta-D-glucose
-
-
17.5
-
1-O-vanilloyl-beta-D-glucose
-
-
4
-
1-O-Veratroyl-beta-D-glucose
-
-
5.5
-
3,6-di-O-galloyl-beta-D-glucose
-
-
6
-
4-O-digalloyl-1,2,3,6-tetra-O-galloyl-beta-D-glucose
-
-
-
4.7
-
6-O-galloyl-beta-D-glucose
-
-
4.1
-
chlorogenic acid
-
-
2.3
-
ethyl gallate
-
-
0.7
-
m-digallic acid
-
tannase II
0.99
-
m-digallic acid
-
-
2
-
m-digallic acid
-
tannase I
0.41
-
Methyl 3,4,5-trihydroxybenzoate
-
at 60C
0.433
-
methyl gallate
-
free enzyme, in citrate buffer (50 mM, pH 5.5), at 30C
0.529
-
methyl gallate
-
Ca alginate-immobilized enzyme, in citrate buffer (50 mM, pH 5.5), at 30C
0.62
-
methyl gallate
B3Y018
at pH 8.0
0.78
-
methyl gallate
-
enzyme produced under solid-state fermentation, at pH 7.0, 30C
0.86
-
methyl gallate
-
-
0.95
-
methyl gallate
-
-
1.6
-
methyl gallate
-
-
1.7
-
methyl gallate
-
tannase I
1.82
-
methyl gallate
-
at 45C, in 50 mM citrate buffer at pH 5.0
1.9
-
methyl gallate
C7F6Y1
at pH 2.0, 30C
2.06
-
methyl gallate
-
at 40C, in 50 mM citrate buffer at pH 5.0
3.5
-
methyl gallate
B7VFD0, -
recombinant tannase, at 30C, pH 6.0
3.7
-
methyl gallate
C7EDT0
pH and temperature not specified in the publication
4.06
-
methyl gallate
-
at 50C, in 50 mM citrate buffer at pH 5.0
4.35
-
methyl gallate
-
at 55C, in 50 mM citrate buffer at pH 5.0
4.4
-
methyl gallate
B7VFD0, -
endogenous tannase, at 30C, pH 6.0
4.47
-
methyl gallate
-
at 60C, in 50 mM citrate buffer at pH 5.0
4.78
-
methyl gallate
-
pH 5.0, 45C
4.94
-
methyl gallate
-
at 20C, in 50 mM citrate buffer at pH 5.0
5.06
-
methyl gallate
-
at 35C, in 50 mM citrate buffer at pH 5.0
5.11
-
methyl gallate
-
at 25C, in 50 mM citrate buffer at pH 5.0
5.17
-
methyl gallate
-
at 30C, in 50 mM citrate buffer at pH 5.0
6.2
-
methyl gallate
-
tannase II
7.41
-
methyl gallate
-
enzyme produced under submerged fermentation, at pH 7.0, 30C
12.05
-
methyl gallate
-
at 65C, in 50 mM citrate buffer at pH 5.0
14
-
methyl gallate
Penicillium variabile
-
in 0.5 M citrate phosphate buffer, pH 5.0, at 50C
2.05
-
propyl gallate
-
-
2.4
-
propyl gallate
-
-
7.69
-
propyl gallate
-
pH 5.0, 45C
12
-
propyl gallate
Penicillium variabile
-
in 0.5 M citrate phosphate buffer, pH 5.0, at 50C
16.94
-
pyrogallol
-
pH 5.0, 45C
0.000011
-
Tannic acid
-
free enzyme, pH 5.0, 30C
0.000041
-
Tannic acid
-
immobilized enzyme, pH 6.0, 40C
0.00061
-
Tannic acid
-
pH 5.5, 60C
0.048
-
Tannic acid
-
-
0.05
-
Tannic acid
-
-
0.14
-
Tannic acid
B7VFD0, -
endogenous tannase, at 30C, pH 6.0
0.17
-
Tannic acid
B7VFD0, -
recombinant tannase, at 30C, pH 6.0
0.21
-
Tannic acid
-
pH 5.0, 40C
0.23
-
Tannic acid
-
at 60C
0.28
-
Tannic acid
-
-
0.28
-
Tannic acid
-
-
0.4
-
Tannic acid
-
free enzyme, in citrate buffer (50 mM, pH 5.5), at 30C
0.49
-
Tannic acid
-
enzyme produced under submerged fermentation, at pH 7.0, 30C
1.05
-
Tannic acid
-
isozyme TAH I, pH 5.5, 20C
1.4
-
Tannic acid
-
enzyme produced under solid-state fermentation, at pH 7.0, 30C
1.51
-
Tannic acid
-
isozyme TAH II, pH 5.5, 20C
3.57
-
Tannic acid
-
purified enzyme
5.5
-
Tannic acid
-
at pH 5.5, 37C
14.01
-
Tannic acid
-
pH 5.0, 45C
23.75
-
Tannic acid
-
Ca alginate-immobilized enzyme, in citrate buffer (50 mM, pH 5.5), at 30C
32
-
Tannic acid
Penicillium variabile
-
pH 5.0, 50C
32
-
Tannic acid
Penicillium variabile
-
in 0.5 M citrate phosphate buffer, pH 5.0, at 50C
0.00061
-
tannin
-
-
-
71.4
-
methyl gallate
-
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
17.02
-
methyl gallate
-
at 20C, in 50 mM citrate buffer at pH 5.0
52.48
-
methyl gallate
-
at 25C, in 50 mM citrate buffer at pH 5.0
60.99
-
methyl gallate
-
at 35C, in 50 mM citrate buffer at pH 5.0
78.01
-
methyl gallate
-
at 30C, in 50 mM citrate buffer at pH 5.0
580.1
-
methyl gallate
-
at 40C, in 50 mM citrate buffer at pH 5.0
601.4
-
methyl gallate
-
at 45C, in 50 mM citrate buffer at pH 5.0
1109
-
methyl gallate
-
at 50C, in 50 mM citrate buffer at pH 5.0
1364
-
methyl gallate
-
at 55C, in 50 mM citrate buffer at pH 5.0
1564
-
methyl gallate
-
at 60C, in 50 mM citrate buffer at pH 5.0
2611
-
methyl gallate
-
at 65C, in 50 mM citrate buffer at pH 5.0
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.112
-
methyl gallate
B7VFD0, -
recombinant tannase, at 30C, pH 6.0
24430
0.127
-
methyl gallate
B7VFD0, -
endogenous tannase, at 30C, pH 6.0
24430
3.45
-
methyl gallate
-
at 20C, in 50 mM citrate buffer at pH 5.0
24430
10.26
-
methyl gallate
-
at 25C, in 50 mM citrate buffer at pH 5.0
24430
12.06
-
methyl gallate
-
at 35C, in 50 mM citrate buffer at pH 5.0
24430
15.08
-
methyl gallate
-
at 30C, in 50 mM citrate buffer at pH 5.0
24430
216.7
-
methyl gallate
-
at 65C, in 50 mM citrate buffer at pH 5.0
24430
273.5
-
methyl gallate
-
at 50C, in 50 mM citrate buffer at pH 5.0
24430
282
-
methyl gallate
-
at 40C, in 50 mM citrate buffer at pH 5.0
24430
313.7
-
methyl gallate
-
at 55C, in 50 mM citrate buffer at pH 5.0
24430
330
-
methyl gallate
-
at 45C, in 50 mM citrate buffer at pH 5.0
24430
350.2
-
methyl gallate
-
at 60C, in 50 mM citrate buffer at pH 5.0
24430
0.064
-
Tannic acid
B7VFD0, -
recombinant tannase, at 30C, pH 6.0
16878
0.078
-
Tannic acid
B7VFD0, -
endogenous tannase, at 30C, pH 6.0
16878
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.5
-
Ag+
-
40C
0.49
-
Ba2+
-
40C
0.59
-
CaCl2
-
-
0.45
-
Gallic acid
B7VFD0, -
endogenous tannase
0.57
-
Hg2+
-
40C
8.25
-
Zn2+
-
40C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.031
-
-
crude extract, pH 5.0, 45C
0.084
-
C7EDT0
crude extract, pH and temperature not specified in the publication
0.1602
-
-
6 step purified enzyme
0.18
-
-
purified enzyme, substrate catechin gallate
0.31
-
-
crude extract, at pH 5.5, 37C
0.43
-
-
purified enzyme, substrate epicatechin gallate
0.575
-
-
crude extract, pH 5.5, 50C
0.64
-
-
purified enzyme, substrate epigallocatechin gallate
0.84
-
-
purified enzyme, substrate tannic acid
0.87
-
-
purified enzyme, substrate gallic acid methyl ester
1.13
-
-
purified enzyme, substrate gallocatechin gallate
1.6
-
-
pH 6.0
1.91
-
-
after 61.61fold purification, pH 5.0, 45C
2.7
-
Hyalopus sp.
-
fermented broth, in 0.2 M acetate buffer, pH 5.5, at 40C, for 30 min
5.6
-
-
purified native enzyme
6.3
-
Hyalopus sp.
-
2.33fold purified enzyme, in 0.2 M acetate buffer, pH 5.5, at 40C, for 30 min
6.49
-
-
after 21fold purification, at pH 5.5, 37C
6.8
-
-
methyl gallate, activity increases 17fold, when the cells are grown in the presence of methyl gallate and 36fold in the presence of tannic acid
7.5
-
B3Y018
crude extract, at pH 8.0
13.63
-
C7EDT0
after 162fold purification, pH and temperature not specified in the publication
14.65
-
-
immobilized enzyme
15.27
-
Penicillium variabile
-
crude filtrate, in 0.5 M citrate phosphate buffer, pH 5.0, at 50C
20
-
-
purified enzyme, in 100 mM sodium acetate, pH 5.0, 30% (w/v) diglyme, at 4C
22.85
-
-
after 39.74fold purification, pH 5.5, 50C
33.7
-
-
crude extract
61.8
-
-
purified isozyme TAH I
72.2
-
-
free enzyme
78
-
-
purified enzyme
82.2
-
-
purified isozyme TAH II
84.34
-
B3Y018
after 11.25fold purification, at pH 8.0
86
-
-
3 step purified enzyme
88.3
-
-
after 2.62fold purification
92
-
Candida sp.
-
8 step purified enzyme
118.8
-
-
3 step purification
135
-
-
5 step purification
170
-
-
purified enzyme
250
-
-
commercial preparation
264.5
-
-
enzyme produced under solid-state fermentation, after 153fold purification, at pH 7.0, 30C
355.6
-
-
purified enzyme
436.7
-
C7F6Y1
crude extract, pH 2.0, 30C
489
-
-
crude extract
2055
-
Penicillium variabile
-
purified native enzyme
2055
-
Penicillium variabile
-
after 135fold purification, in 0.5 M citrate phosphate buffer, pH 5.0, at 50C
2067
-
-
enzyme produced under submerged fermentation, after 477fold purification, at pH 7.0, 30C
2762
-
C7F6Y1
after 6.32fold purification, pH 2.0, 30C
9550
-
-
19.5fold purified enzyme
49330
-
-
pH 5.0, 30C
additional information
-
Penicillium variabile
-
activity at different fermentation conditions, overview
additional information
-
-
-
additional information
-
-
activity depending on growth substrate
additional information
-
-
enzyme activity during cell growth in a fermenter culture, production kinetics
additional information
-
-
-
additional information
-
-
enzyme activity on different substrate for solid-state fermentation, overview
additional information
-
-
activity of extracellular and intracellular enzymes
additional information
-
-
-
additional information
-
-
paper chromatographic detection method development
additional information
-
-
the crude extract initially has a specific activity of 5.2 IU/mg. The 46fold purified enzyme has a specific activity of 238.14 IU/mg
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
-
-
two pH optima are observed for maximal activity, one at pH 2.0 and the other at a pH 8.0
2
-
C7F6Y1
two pH optima, pH 2.0 and pH 8.0, are recorded
4
-
-
a minor secondary peak at pH 4.0 is found in both enzymes produced under solid-state and submerged fermentations with 70% of tannase activation
4.3
5
-
potassium phosphate/citrate buffer
4.5
6.5
-
purified enzyme, 70% of maximal activity at pH 4.5, maximal activity at pH 5.5, and 80% of maximal activity at pH 6.5
4.5
-
-
optimal pH for enzyme production
4.5
-
-
immobilized enzyme
5
5.5
-
methyl gallate as substrate
5
6
-
submerged fermentation of Aspergillus
5
6.5
-
solid-state fermentation of Aspergillus
5
-
Penicillium variabile
-
assay at
5
-
-
free enzyme
5
-
-
esterase activity
5
-
-
maximal cell growth and enzyme production in vivo
5
-
-
intra- and extracellular enzyme form
5
-
-
optimal pH for enzyme production
5
-
-
assay at
5
-
Penicillium variabile
-
-
5
-
-
enzyme from co-culture with Rhizopus oryzae, the tannase needs an acidic environment to be active
5
-
-
enzyme from co-culture with Aspergillus foetidus, the tannase needs an acidic environment to be active
5
-
Penicillium variabile
-
-
5
-
-
intracellular enzyme of the submerged fermentation
5.5
6.5
-
liquid-surface fermentation of Aspergillus
5.5
-
-
assay at
5.5
-
-
strain PKL-104
5.5
-
-
isozymes TAH I and TAH II
5.5
-
C7EDT0
-
5.5
-
-
at 37C
5.5
-
-
extracellular enzyme produced in the solid-state fermentation
5.5
-
-
free enzyme
5.7
6
B7VFD0, -
endogenous and recombinant tannases
5.8
-
-
maximal enzyme activity in vitro with partially purified enzyme
6
-
-
immobilized enzyme
6
-
-
optimal pH value for enzyme production in culture
6
-
-
tannase activity, strain N888
6
-
-
at 30C, using methyl 3,4,5-trihydroxybenzoate as substrate
6
-
-
maximum tannase activity at pH 6.0
6
-
-
at 30C
6
-
-
pH optimum for both enzymes produced under solid-state and submerged fermentations
6
-
Candida sp.
-
-
6
-
-
pI 4.3
6.4
-
E7D7J5
-
6.5
-
Hyalopus sp.
-
-
6.6
-
-
optimal growth and enzyme production pH value
7
-
-
purified recombinant tannase
8
-
-
two pH optima are observed for maximal activity, one at pH 2.0 and the other at a pH 8.0
8
-
C7F6Y1
two pH optima, pH 2.0 and pH 8.0, are recorded
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1
7
C7F6Y1
the enzyme records a significant level of activity even at a pH of 1.0, however, the enzyme activity declines rapidly at pH 3.0-4.0 and is almost nil at a pH of 7.0
2
6
-
at pH 2.0 exhibits a relative activity of about 45%
2
8
-
extracellular enzyme produced in the solid-state fermentation
3
7
-
in vivo enzyme production
3
8
Penicillium variabile
-
activity range
3
8
Penicillium variabile
-
-
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
3
9
-
maximal activity at pH 5.0, 40% of maximal activity at pH 6.0
3.5
6
-
activity of the partially purified enzyme
3.5
6.5
-
cell growth and enzyme production in vivo
3.5
7
-
partially purified enzyme
4
5
-
tannase activity is greatly decreased below pH 4.0 and above pH 5.0
4
6.3
-
half-maximal acivities at pH 4.0 and pH 6.3, inactive below pH 3.8 and above pH 7.8
4
7
-
intracellular enzyme of the submerged fermentation
4.5
5.5
-
extracellular enzyme of the submerged fermentation
5
7
-
pH 5.0 and pH 7.0: 50-60% of the maximal activity
6
8
-
pH 6: 53% of the maximal activity, pH 8: 85% of the maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
isozyme TAH II
25
-
-
isozyme TAH I
30
-
-
free enzyme; immobilized enzyme
30
-
-
optimal growth and enzyme production temperature
30
-
-
independent of fermentation process
30
-
-
in vivo assay at
30
-
C7F6Y1
-
35
40
B7VFD0, -
endogenous and recombinant tannases
35
40
-
activation energy of 24.3 kJ per mol
37
-
-
optimal temperature for enzyme production in culture, assay at
40
-
-
immobilized enzyme
40
-
-
assay at
40
-
-
in vitro assay at
40
-
-
enzyme from a commercial strain
40
-
-
enzyme from co-culture with Rhizopus oryzae
40
-
-
enzyme from co-culture with Aspergillus foetidus
40
-
-
purified recombinant tannase
40
-
-
maximum tannase activity at 40C
40
-
C7EDT0
-
40
-
-
free enzyme, activation energy 6.75 kcal per mol
50
60
-
enzyme produced under submerged fermentation
50
-
Penicillium variabile
-
assay at
50
-
-
extracellular enzyme form
50
-
Penicillium variabile
-
-
50
-
-
assay at
50
-
Penicillium variabile
-
-
50
-
Candida sp.
-
-
55
-
-
immobilized enzyme, activation energy 5.77 kcal per mol
60
-
-
strain PKL-104
60
-
-
intracellular enzyme form
60
-
Hyalopus sp.
-
-
60
-
-
with 0.1 M citrate buffer, pH 5.5
60
-
-
at a methyl gallate concentration of 4.4 mM
60
-
-
enzyme produced under solid-state fermentation
60
-
-
extracellular enzyme produced in the solid-state fermentation and in the submerged fermentation
70
-
-
strain N888
70
-
-
intracellular enzyme of the submerged fermentation
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
80
C7F6Y1
the enzyme activity declines markedly along with increases in temperature above 60C
20
45
-
active between these temperatures
20
60
-
at 20C exhibits a relative activity of 10%
20
60
-
20C: 58% of the maximal activity, 60C: 2% of the maximal activity
20
70
-
maximal activity at 30C, 50% of maximal activity at 50C
20
80
-
purified enzyme, 20% of maximal activity at 20C and at 80C, 50% of maximal activity at 40C and at 65C, maximal activity at 50C
25
75
-
immobilized enzyme, 25C: 40% of the maximal activity, 75C: 18% of the maximal activity. Free enzyme, 25C: 57% of the maximal activity, 75C: 10% of the maximal activity
25
80
Penicillium variabile
-
activity range
25
80
Penicillium variabile
-
-
30
90
-
markedly reduced activity above 70C
additional information
-
-
temperature profile of the isozymes
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.8
-
-
strain N888
3.8
-
-
isoelectric focusing
4.4
-
C7F6Y1
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Lactobacillus plantarum CECT 748(T)
-
-
-
Manually annotated by BRENDA team
-
submerged fermentation culture
Manually annotated by BRENDA team
-
intracellular tannase is tightly bound with the mycelium
Manually annotated by BRENDA team
-
mycelium-bound tannase
Manually annotated by BRENDA team
Aspergillus niger MTCC 2425
-
-
-
Manually annotated by BRENDA team
Caesalpinia coriaria
-
-
Manually annotated by BRENDA team
Caesalpinia coriaria
-
-
Manually annotated by BRENDA team
additional information
Penicillium variabile
-
optimization of fermentation conditions, statistics
Manually annotated by BRENDA team
additional information
-
culture methods, overview
Manually annotated by BRENDA team
additional information
-
culture conditions
Manually annotated by BRENDA team
additional information
-
modified solid-state fermentation
Manually annotated by BRENDA team
additional information
-
from submerged or solid-state cultures with higher enzyme activity in the latter
Manually annotated by BRENDA team
additional information
-
from solid-state culture, optimal on minimal medium containing 0.2% w/v glucose and 0.7% w/v tannic acid at 37 C and pH 6.0 in the absence of O2
Manually annotated by BRENDA team
additional information
-
from submerged or solid-state cultures with higher enzyme activity in the latter
Manually annotated by BRENDA team
additional information
-
optimization of culture conditions for tannase production, presence of additional carbon sources like maltose, glucose, and sucrose at 0.1% w/v concentration in the tannic acid medium is found to be effective for growth of the organism and inductive for enzyme production, though tannase synthesis is inhibited in maltose and arabinose, (NH4)2HPO4 as nitrogen source results in high enzyme production rates, overview
Manually annotated by BRENDA team
additional information
-
co-culture with Rhizopus oryzae, solid-state fermentation on tannin rich substrates
Manually annotated by BRENDA team
additional information
-
co-culture with Aspergillus foetidus, solid-state fermentation on tannin rich substrates
Manually annotated by BRENDA team
additional information
Aspergillus foetidus GMRB 013 MTCC 3557
-
co-culture with Rhizopus oryzae, solid-state fermentation on tannin rich substrates
-
Manually annotated by BRENDA team
additional information
Aspergillus niger Aa-20
-
from submerged or solid-state cultures with higher enzyme activity in the latter
-
Manually annotated by BRENDA team
additional information
Aureobasidium pullulans DBS66
-
optimization of culture conditions for tannase production, presence of additional carbon sources like maltose, glucose, and sucrose at 0.1% w/v concentration in the tannic acid medium is found to be effective for growth of the organism and inductive for enzyme production, though tannase synthesis is inhibited in maltose and arabinose, (NH4)2HPO4 as nitrogen source results in high enzyme production rates, overview
-
Manually annotated by BRENDA team
additional information
Rhizopus oryzae RO IIT RB-13
-
co-culture with Aspergillus foetidus, solid-state fermentation on tannin rich substrates
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
5fold lower production level in culture than the intracellular form
-
Manually annotated by BRENDA team
Aspergillus aculeatus DBF 9
-
5fold lower production level in culture than the intracellular form
-
-
Manually annotated by BRENDA team
Aspergillus awamori BTMFW032
-
;
-
-
Manually annotated by BRENDA team
Aspergillus heteromorphus MTCC 8818
-
-
-
-
Manually annotated by BRENDA team
Bacillus licheniformis KBR 6
-
;
-
-
Manually annotated by BRENDA team
Lactobacillus sp. ASR-S1
-
-
-
-
Manually annotated by BRENDA team
-
5fold higher production level in culture than the extracellular form
Manually annotated by BRENDA team
-
intracellular tannase is tightly bound with the mycelium
Manually annotated by BRENDA team
Aspergillus aculeatus DBF 9
-
5fold higher production level in culture than the extracellular form
-
Manually annotated by BRENDA team
-
mucous membrane
Manually annotated by BRENDA team
-
intracellular enzyme
Manually annotated by BRENDA team
Aspergillus aculeatus DBF 9
-
intracellular enzyme
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45000
-
P78581
purified tannase with 2-mercaptoethanol, SDS-PAGE
50000
-
B3Y018
SDS-PAGE
50700
-
B3Y018
deduced from the amino acid sequence
55000
-
E7D7J5
gel filtration
61000
-
B7VFD0, -
mature enzyme, calculated from the ORF
100000
-
P78581
purified tannase without 2-mercaptoethanol, SDS-PAGE
149800
-
-
PAGE
150000
-
-
purified enzyme
150000
-
-
can exist as tetramer or dimer, gel fitration
155000
-
-
isozymes TAH I and TAH II, gel filtration
163000
-
-
gel filtration
186000
-
-
-
186000
-
-
glycoprotein containing 43% sugars, nondenaturing PAGE
192300
-
-
sedimentation equilibrium
194000
-
-
sedimentation diffusion
200000
-
-
gel filtration
230000
-
-
gel filtration
230000
-
C7F6Y1
gel filtration
250000
-
Candida sp.
-
gel filtration
290000
-
-
strain AO1, glycoprotein containing 22.7% sugars, a hetero-octamer with four pairs of two subunits, sedimentation equilibrium
300000
-
-
can exist as tetramer or dimer, gel fitration
302000
-
-
gel filtration
310000
-
-
-
310000
-
Penicillium variabile
-
gel filtration
310000
-
-
strain AO1, glycoprotein containing 22.7% sugars, a hetero-octamer with four pairs of two subunits, gel filtration
320000
-
B7VFD0, -
native endogenous and recombinant tannases, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 80000-85000, strain N888
?
-
x * 102000, SDS-PAGE, x * 83000, SDS-PAGE
?
-
x * 90000, SDS-PAGE, x * 180000, SDS-PAGE
?
-
x * 168000, SDS-PAGE
?
-
x * 100000, SDS-PAGE, x * 31000 + x * 34000, SDS-PAGE after treatment with N-glycosidase F, x * 90000, mass spectrometry
?
-
x * 40000, isozyme TAH I, SDS-PAGE, x * 46000, isozyme TAH II, SDS-PAGE
?
-
x * 87300, SDS-PAGE
?
-
x * 102000 + x * 83000
?
-
x * 101000, SDS-PAGE
?
-
x * 102000, enzyme produced under solid-state fermentation, SDS-PAGE; x * 105000, enzyme produced under submerged fermentation, SDS-PAGE
?
C7EDT0
x * 90000, SDS-PAGE
?
-
x * 59000, SDS-PAGE
?
Aspergillus awamori MTCC9299
-
x * 101000, SDS-PAGE
-
?
Aspergillus niger MTCC 2425
-
x * 102000, SDS-PAGE, x * 83000, SDS-PAGE
-
?
Enterobacter sp. KPJ103
-
x * 90000, SDS-PAGE
-
dimer
Penicillium variabile
-
2 * 158000, SDS-PAGE
dimer
Candida sp.
-
2 * 120000, SDS-PAGE
dimer
-
2 * 75000, SDS-PAGE, can exist as dimer or tetramer
dimer
-
2 * 53000, SDS-PAGE
dimer
Aspergillus niger LCF 8
-
2 * 53000, SDS-PAGE
-
dimer
Candida sp. K-1
-
2 * 120000, SDS-PAGE
-
dimer
Penicillium variabile IARI 2031
-
2 * 158000, SDS-PAGE
-
heterodimer
P78581
1 * 33000 + 1 * 30000, purified tannase digested with N-glycosidase F and loaded with 2-mercaptoethanol, SDS-PAGE
heterotetramer
-
2 * 45800 + 2 * 52000, SDS-PAGE
homodimer
Penicillium variabile
-
2 * 155000, gel filtration; 2 * 158000, SDS-PAGE
homodimer
Penicillium variabile IARI 2031
-
2 * 155000, gel filtration; 2 * 158000, SDS-PAGE
-
homohexamer
-
6 * 37800, SDS-PAGE
homohexamer
Aspergillus awamori BTMFW032
-
6 * 37800, SDS-PAGE; 6 * 37800, SDS-PAGE
-
homotetramer
B7VFD0, -
4 * 80000, denatured endogenous and recombinant tannases, SDS-PAGE. 4 * 55000, deglycosylated endogenous and recombinant tannases, SDS-PAGE
homotrimer
-
3 * 50000, SDS-PAGE
monomer
B3Y018
1 * 50000, 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
tetramer
-
4 * 75000, SDS-PAGE, can exist as dimer or tetramer
trimer
-
3 * 45000, SDS-PAGE
trimer
-
1 * 50000 + 1 * 75000 + 1 * 100000, SDS-PAGE
trimer
Aspergillus niger GH1
-
1 * 50000 + 1 * 75000 + 1 * 100000, SDS-PAGE
-
monomer
E7D7J5
1 * 55000, SDS-PAGE
additional information
-
the native enzyme undergoes dissociation into inactive subunits of equal size by treatment with guanidine hydrochloride
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
14.2% carbohydrate content
glycoprotein
-
-
side-chain modification
-
glycoprotein, 25.4% carbohydrate content
glycoprotein
-
-
glycoprotein
-
contains 43% sugar
glycoprotein
-
-
side-chain modification
-
glycoprotein, containg 43% sugars
side-chain modification
Aspergillus niger LCF 8
-
glycoprotein, containg 43% sugars
-
side-chain modification
-
glycoprotein, tannase I contains 5.4% and tannase II contains 5.4% neutral sugars, glucose-mannose-galactose, respectively
glycoprotein
-
-
side-chain modification
Candida sp.
-
glycoprotein, 64% carbohydrates, contains 62% neutral sugars, mannose and galactose, and 2.2% hexosamines
side-chain modification
Candida sp. K-1
-
glycoprotein, 64% carbohydrates, contains 62% neutral sugars, mannose and galactose, and 2.2% hexosamines
-
glycoprotein
-
-
glycoprotein
-
carbohydrate content of 50%
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
-
-
stability at pH 2.0 is maintained for 24 h
2
-
C7F6Y1
the enzyme is stable (99%) over a relatively long duration of incubation (up to 24 h) only at pH 2.0. At other pH levels, the enzyme is not stable
3
10
Penicillium variabile
-
the enzyme shows 60% residual activity at pH 3.0, almost 100% stability in pH range of 4.0-6.0 for 24 h, at pH 10.0 crude and purified tannase retain 19.7% and 15.3% residual activity for 24 h, immobilized tannase retains 24.6% residual activity at this pH even after 24 h
3
5
-
24 h, 70% residual activity
3
5
-
24 h, 95% residual activity
3
6
-
in the pH range 3.0-5.0, tannase proves to be significantly stable, showing half-lives ranging from 131 to 372 h. At pH 6.0 and 5.5 half-lives of 632 h and 607 h, respectively
3
7.5
-
stable for 12 h at 5C
3.5
8.5
-
purified enzyme, 40% of maximal activity at pH 3.5, maximal activity at pH 5.5, and 20% of maximal activity at pH 8.5
3.5
9
Candida sp.
-
pH 3.5: 80% of the maximal activity, pH 7.5: 40% of the maximal activity
3.5
-
-
unstable below
4
5
-
the enzyme retained around 80% of control activity when maintained for 60 h at pH 4.0 or 5.0. Increasing pH values (6.0-10.0) result in decreased stability of the enzyme, with a half-life of 20 h at pH 7.0
4
6.5
-
stable at 16C
4.5
6
-
liquid-surface fermentation of Aspergillus; submerged fermentation of Aspergillus
4.5
6
-
stable for 25 h at 5C
4.5
6.5
-
solid-state fermentation of Aspergillus
4.5
7.5
-
loss of 10-30% activity of TAH I and TAH II at '5C and 4C
5
5.5
-
methyl gallate as substrate, stable in 0.01 M acetate buffer, at 5C, outside this range the activity increases rapidly
5
7
B7VFD0, -
endogenous and recombinant tannases
5
7
-
the stability pH is 6.0 at 4C for 24 h for both purified tannases maintaining 100% of enzymatic activity. Submerged fermentation tannase supports 90-100% enzymatic activity at pH 5.0-7.0. The solid-state fermentation tannase at pH values of 5.0 and 6.0, supports 85-100% activity
5
8
Hyalopus sp.
-
-
5
-
-
24 h, 100% residual activity
5
-
-
24 h, 48% residual activity
5
-
-
greatest stability after preincubation at 30C for 60 min or 24 h
6
8
-
24 h, 60% residual activity
6
8
-
purified enzyme
6
-
-
24 h, 80% residual activity
6
-
-
24 h, 38% residual activity
6
-
-
24 h, 100% residual activity
7
-
-
24 h, 65% residual activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
-
-
42% of the maximal activity
4
45
-
stable between
20
30
-
isozymes TAH I and TAH II, stable
20
40
-
liquid-surface fermentation of Aspergillus
20
50
-
purified enzyme, fully stable
20
60
-
immobilized enzyme, 87% remaining activity after 1 h at 60C
20
60
-
solid-state fermentation of Aspergillus; submerged fermentation of Aspergillus
22
90
-
the enzyme is very stable in the temperature range of 22-50C for up to 70 h and has a half-life of about 72 h at 90C
25
90
Penicillium variabile
-
at 25C crude and immobilized enzyme show 78% and 81% relative activity while purified tannase has a relative activity of 70% at this temperature, at 80C more than 50% relative activity is observed in crude and immobilized tannase while 45% in purified form, at 90C crude and immobilized enzyme retain 23% and 31% relative activity while purified tannase shows a relative activity of only 11%
30
45
-
immobilized enzyme, 30% remaining activity after 1 h at 60C
30
45
-
at 30C the enzyme is totally stable between pH 3.0 and 8.0 for 2 h, the enzyme is stable up to 45C
30
50
-
1 h, 85% residual activity
30
50
B7VFD0, -
endogenous and recombinant tannases
30
70
C7F6Y1
the enzyme is stable only at 30C for 24 h, retaining about 60% activity. The residual activity is 72% at 40C for 2 h, 54% at 50C for 6 h, 53% at 60C for 4 h, and 72% at 70C for 1 h
30
-
-
stable up to for 1 h
30
-
-
1 h, 61% residual activity
30
-
-
stable up to
40
50
-
isozymes TAH I and TAH II, loss of 50-80% activity
40
50
E7D7J5
the enzyme is stable below 40C, as after prolonged incubation time it does not show obvious loss of activity under the standard conditions. However, the enzyme keeps only 47% of its activity after incubation at 50C for 12 h
40
60
-
the enzyme is stable at temperatures between 40 and 60C but loses all activity at 90-100C
40
-
-
stable for 20 min
40
-
-
stable up to
40
-
-
1 h, 100% residual activity
40
-
-
1 h, 90% residual activity
40
-
-
inactivation of purified enzyme after 255 min
40
-
-
significant decrease in thermal stability at temperatures above 40C
40
-
Candida sp.
-
stable up to
40
-
-
the intracellular enzyme of the submerged fermentation is highly unstable above
45
55
B3Y018
the enzyme retains more than 50% activity between 25 and 45C but the activity drops off markedly above 45C
45
-
-
95% stability up to
50
60
Hyalopus sp.
-
60C: heat stable for 10 min. 50C: heat stable for 30 min, loses only 4% of its activity even after 60 min
50
70
-
half-lives of the enzyme at 50, 60, and 70C are 281, 25, and 4 min, respectively
50
-
-
stable up to, extracellular enzyme form
50
-
-
1 h, 98% residual activity
50
-
-
1 h, 73% residual activity
50
-
-
the enzyme is inactivated after 30 min at 50C
50
-
-
88% of the activity retains, extracellular enzyme produced in the solid-state fermentation
50
-
-
heat-denaturation above
50
-
-
half-life of free enzyme: 90 min, half-life of immobilized enzyme: 120 min
55
-
-
activity completely lost after 20 min
60
70
-
solid-state fermentation tannase and submerged fermentation tannase are stable at 60C for 1 h incubation retaining around 90% of activity. Both purified tannases lose the activity at 80C, nevertheless, the submerged fermentation tannase only loses 20% of activity at 70C for 1 h incubation and solid-state fermentation tannase retaining 30% of activity at the same condition
60
-
-
stable up to, intracellular enzyme form
60
-
-
1 h, 70% residual activity
60
-
-
1 h, 100% residual activity
60
-
-
1 h, 78% residual activity
60
-
-
inactivation of purified enzyme after 105 min
60
-
C7EDT0
the enzyme retains 20% of its activity at 60C
60
-
-
stable up to
60
-
-
83% of the activity retains, extracellular enzyme produced in the solid-state fermentation
60
-
-
half-life of free enzyme: 18 min, half-life of immobilized enzyme: 40 min
65
-
-
purified enzyme, 50% of maximal activity
65
-
-
inactivation of purified enzyme after 75 min
70
80
-
purified enzyme, 20% of maximal activity
70
80
-
complete inactivation
70
-
-
1 h, 13% residual activity
70
-
-
1 h, 67% residual activity
70
-
-
use of heat mutant results in increased thermostability with optimal activity. The mutagenesis confers increased thermostability up to 70C till 60 min, with 82.7% residual tannase activity
70
-
-
midpoint of thermal inactivation at 70C after 60 min of exposure
70
-
Candida sp.
-
rapidly modified and loss of activity
70
-
-
the activity is rapidly lost
70
-
-
half-life of free enzyme: 8 min at, half-life of immobilized enzyme: 25 min
85
-
-
activity completely lost after 10 min
90
-
-
purified enzyme, inactivation
additional information
-
-
temperature profile of the isozymes
additional information
-
-
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
salt-tolerant enzyme, stable up to 2 M NaCl, and 82% remaining activity in presence of 3 M NaCl
-
a mixture of tannic acid and PEG 6000 protect the enzyme during purification
-
the glyoxyl agarose gel-immobilized enzyme is stabilized 500-1000fold with regard to one-point covalent immobilized derivatives
-
the immobilisation of tannase by multipoint covalent attachment on glyoxyl agarose strongly increases the stability of the enzyme in the presence of 1-propanol (e.g. 10fold more stable than a tannase derivative obtained by a very mild immobilisation on CNBr-activated agarose)
-
the tannase can successfully be immobilized on Amberlite IR where it retains about 85% of the initial catalytic activity even after the ninth cycle of its use
Penicillium variabile
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-mercaptomethanol
Penicillium variabile
-
39.6% residual activity at 1 mM
Acetone
Penicillium variabile
-
49% residual activity after 60 min at 20% (v/v)
Acetone
C7F6Y1
about 70% activity after 1 h at 10% (v/v)
Acetone
-
130.37% activity at 1% (v/v)
Acetone
Aspergillus awamori BTMFW032
-
about 70% activity after 1 h at 10% (v/v)
-
Acetone
Penicillium variabile IARI 2031
-
49% residual activity after 60 min at 20% (v/v)
-
acetonitrile
C7F6Y1
about 85% activity after 1 h at 10% (v/v)
acetonitrile
-
149.85% activity at 1% (v/v)
acetonitrile
Aspergillus awamori BTMFW032
-
about 85% activity after 1 h at 10% (v/v)
-
benzene
-
116.7% activity at 1% (v/v)
benzene
C7F6Y1
about 45% activity after 1 h at 10% (v/v)
Brij-35
C7F6Y1
the enzyme is not stable in the presence of Brij-35, with less than 82% residual activity at 0.1-1% (v/v)
Butanol
-
115.5% residual activity at 5% (v/v)
Butanol
C7F6Y1
about 70% activity after 1 h at 10% (v/v)
Butanol
Aspergillus awamori BTMFW032
-
about 70% activity after 1 h at 10% (v/v)
-
Butanol
Aspergillus heteromorphus MTCC 8818
-
115.5% residual activity at 5% (v/v)
-
carbon tetrachloride
Penicillium variabile
-
57% residual activity after 60 min at 60% (v/v)
chloroform
C7F6Y1
about 60% activity after 1 h at 10% (v/v)
DMSO
-
122.4% residual activity at 5% (v/v)
DMSO
C7F6Y1
at a 60% concentration of DMSO, the enzyme retains a 61% activity after 24 h
Ethanol
Penicillium variabile
-
35.7% residual activity after 60 min at 60% (v/v)
Ethanol
-
104.4% residual activity at 1% (v/v)
Ethanol
C7F6Y1
about 80% activity after 1 h at 10% (v/v)
Ethanol
-
148.47% activity at 1% (v/v)
Ethanol
Aspergillus awamori BTMFW032
-
about 80% activity after 1 h at 10% (v/v)
-
Ethanol
Aspergillus heteromorphus MTCC 8818
-
104.4% residual activity at 1% (v/v)
-
Ethanol
Penicillium variabile IARI 2031
-
35.7% residual activity after 60 min at 60% (v/v)
-
formaldehyde
Penicillium variabile
-
12% residual activity after 5 min at 20% (v/v)
Glycerol
-
118.2% residual activity at 1% (v/v)
Glycerol
-
138.5% activity at 1% (v/v)
Glycerol
Aspergillus heteromorphus MTCC 8818
-
118.2% residual activity at 1% (v/v)
-
heptane
Penicillium variabile
-
62% residual activity after 60 min at 60% (v/v)
hexane
C7F6Y1
about 80% activity after 1 h at 10% (v/v)
isopropanol
-
106.6% activity at 1% (v/v)
isopropanol
C7F6Y1
about 70% activity after 1 h at 10% (v/v)
isopropanol
-
150% activity at 1% (v/v)
Methanol
-
103.2% residual activity at 1% (v/v)
Methanol
C7F6Y1
about 80% activity after 1 h at 10% (v/v)
Methanol
-
139.57% activity at 1% (v/v)
Methanol
Aspergillus awamori BTMFW032
-
about 80% activity after 1 h at 10% (v/v)
-
n-Butanol
-
140.95% activity at 1% (v/v)
petroleum ether
Penicillium variabile
-
33% residual activity after 60 min at 60% (v/v)
SDS
Penicillium variabile
-
complete inactivation at 1% (w/v)
SDS
-
the enzyme shows considerable stability in the presence of SDS
SDS
Aspergillus foetidus MTCC 6322
-
the enzyme shows considerable stability in the presence of SDS
-
SDS
Penicillium variabile IARI 2031
-
complete inactivation at 1% (w/v)
-
tetrahydrofuran
Penicillium variabile
-
no activity after 5 min at 20% (v/v)
toluene
Penicillium variabile
-
44% residual activity after 60 min at 60% (v/v)
toluene
-
119.4% residual activity at 1% (v/v)
toluene
Aspergillus heteromorphus MTCC 8818
-
119.4% residual activity at 1% (v/v)
-
toluene
Penicillium variabile IARI 2031
-
44% residual activity after 60 min at 60% (v/v)
-
Triton X-100
-
considerable loss in activity in the presence of Triton X-100
Triton X-100
C7F6Y1
at high concentrations of between 0.6% (v/v) (79.06% residual activity) to 1.0% (v/v) (54.26% residual activity), lead to a loss of enzyme stability, although the enzyme is stable at a 0.2% (v/v) concentration (112.2% residual activity) with an enhanced enzyme activity at a 0.4% concentration (171.36% residual activity)
Triton X-100
Aspergillus foetidus MTCC 6322
-
considerable loss in activity in the presence of Triton X-100
-
Tween 60
Penicillium variabile
-
complete inactivation at 1% (v/v)
Tween 60
-
considerable loss in activity in the presence of Tween 60
Tween 60
Aspergillus foetidus MTCC 6322
-
considerable loss in activity in the presence of Tween 60
-
Tween 80
Penicillium variabile
-
complete inactivation at 1% (v/v)
Tween 80
C7F6Y1
Tween 80 leads to an enhanced enzyme activity at up to a 0.6% (v/v) concentration (157.89% residual activity), but displays inhibitory properties at a high concentration of 1.0% (v/v) (83.5% residual activity)
Methanol
Aspergillus heteromorphus MTCC 8818
-
103.2% residual activity at 1% (v/v)
-
additional information
-
effects of organic solvents on propyl gallate production by the enzyme, overview
additional information
Penicillium variabile
-
not affected by Triton X-100
additional information
-
the enzyme shows considerable stability in the presence of commercial detergents such as Sunlight, Rinshakthi and Wheel
additional information
E7D7J5
the enzyme is not influenced by Triton X-100
additional information
Aspergillus foetidus MTCC 6322
-
the enzyme shows considerable stability in the presence of commercial detergents such as Sunlight, Rinshakthi and Wheel
-
additional information
Penicillium variabile IARI 2031
-
not affected by Triton X-100
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
increases in hydrogen peroxide concentrations result in enhanced enzyme activity in the range of 2% (161.1% activity) to 10% (220% activity)
C7F6Y1
715876
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
5C, citrate buffer, pH 5.5 or distilled water, as purified powder or as a solution, maintains activity over 6 months
-
-15C, 3 months
-
4C and 30C, tannase in both crude and crude lyophilized forms, one year, retains more than 60% residual activity
Penicillium variabile
-
shelf-life of crude and crude lyophilized tannase at 4C and at 30C, 70% remaining activity after 365 days, overview
Penicillium variabile
-
4C, in 10 mM acetate buffer (pH 5.5), 3 months, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by ammonium sulfate precipitation followed by ion-exchange chromatography, 19.5folf with 13.5% yield, to homogeneity
-
Sephadex G-200 gel filtration
-
ultrafiltration and Sephadex G-200 gel filtration
C7F6Y1
native enzyme by acetone precipitation and anion exchange chromatography
-
native enzyme from production in a bioreactor by organic solvent precipitation and anion exchange chromatography
-
partial purification by ammonium sulfate precipitation and aqueous two phase extraction with PEG6000
-
ammonium sulfate precipitation and DEAE-cellulose column chromatography (overall purification of 39.74fold with a yield of 19.29%)
-
acetone precipitation and G25 Sephadex gel filtration
-
best at pH 5.5, overview, 51fold
-
isoelectric focusing, High Q column chromatography, High Trap Q column chromatography, High S column chromatography, and Superdex G-200 gel filtration
-
partial purification by HiTrap G25 gel filtration (5.4fold purification and 5.6fold concentration with a recovery yield higher than 90%)
-
to apparent homogeneity, by ultrafiltration, anion-exchange chromatography and gel filtration, with a final yield of 0.3%, 46fold
-
to homogeneity from culture supernatant
-
2 isoenzymes
-
purified from the strain AO1
-
intracellular tannase partially
-
acetone precipitation
-
partially
-
endogenous and recombinant tannases purified by ion-exchange chromatography and gel filtration
B7VFD0, -
613fold
Candida sp.
-
DEAE-cellulose column chromatography and Sephacryl S-200 gel filtration
-
ammonium sulfate precipitation, DEAE cellulose column chromatography, and Sephadex G-100 gel filtration
C7EDT0
to electrophoretic homogeneity through two-step column chromatography
-
partially purified by acetone precipitation, 2.33fold with 79.06% recovery
Hyalopus sp.
-
ammonium sulfate precipitation, Q-Sepharose column chromatography, hydroxylapatite column chromatography, and Mono-Q column chromatography
B3Y018
on affinity column
-
poorly activated Ni-IDA 6% agarose gels column chromatography
-
ammonium sulfate precipitation and ultrafiltration
-
ammonium sulfate precipitation
-
native enzyme by ammonium sulfate fractionation, SDS-PAGE, and anion exchange chromatography 19.3fold to homogeneity
-
native enzyme partially 10fold by ammonium sulfate precipitation followed by anion exchange chromatography
-
native enzyme 135fold by ultrafiltration using 100 kDa molecular weight cut off and gel filtration
Penicillium variabile
-
ultrafiltration and Sephadex G-200 gel filtration
Penicillium variabile
-
1910fold to apparent homogeneity
-
native enzyme by acetone precipitation and anion exchange chromatography
-
partially purified by DEAE-Sepharose column chromatography (21times with 62.5% recovery)
-
Ni-NTA His Bind column chromatography
E7D7J5
native isozymes TAH I and TAH II 7.9fold and 10.5fold, respectively, to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cloned in Escherichia coli JM 109 and expressed in Aspergillus oryzae strain AO1, a tannase low-producing and nitrate reductase-deficient strain
-
expressed in Pichia pastoris strain GS115
P78581
expressed in Arxula adeninivorans strain G1212
-
recombinant ATAN1 gene overexpressed in the auxotrophic mutant strain Arxula adeninivorans G1212 [DELTAatrp1] under the control of the strong, constitutive TEF1 promoter. Expression module assembled in the plasmid pGH101-TEF1-ATAN1 and used to construct YIEC101-TEF1-ATAN1 for transformation of Arxula host cells
B7VFD0, -
1.4 kb purified PCR product of tanLp1 gene cloned into pURI3 vector and transformed into Escherichia coli DH5alpha cells. Recombinant plasmids isolated and overexpressed in Escherichia coli JM109 (DE3)
-
expressed in Escherichia coli DH5alpha
B3Y018
DNA and amino acid sequence determination and analysis, expressionin Escherichia coli strain DH5alpha
Q0KKP0, -
expressed in Escherichia coli BL21(DE3) cells
E7D7J5
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
fall in tannase activity from day 7 to 10 is suggestive of a possible tannase inhibition probably by repression
-
parent strain produces 19.5 U/ml at 72 h of fermentation time in submerged culture. Mutagenesis exerts a positive effect on the strain producing 1.5-2fold increase in tannase production. The heat IV mutant exhibits the highest tannase activity of 38.9 U/ml at 48 h
-
higher titres of tannase with 2.5-2.8fold increase in tannase activity by solid state fermentation
-
addition of MnSO4, ammonium molybdate, or CdSO4 leads to decreased rate of tannase production
-
enzyme production is not induced by the addition of D-glucose (0.05-2% w/v)
-
NH4Cl is the most suitable nitrogen source for maximal tannase production. CaCl2 stimulates tannase production most efficiently. Extract of China green tea is the best source of tannin for high tannase production
-
supplementation with maltose or glycerol inhibits tannase synthesis, which results in lower enzyme activity
-
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
-
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 30C, 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
-
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
-
fall in tannase activity from day 7 to 10 is suggestive of a possible tannase inhibition probably by repression
-
fall in tannase activity from day 7 to 10 is suggestive of a possible tannase inhibition probably by repression
Aspergillus tamarii IMI388810 (B)
-
-
L-cysteine monohydrochloride or DL-threonine are the most potent inhibitors, at pH 5.0, 35C under shaking conditions at 200 rpm. With L-arginine monohydrochloride tannase production is decreased (yield index is 0.78fold)
-
DL-methionine, L-tyrosine, L-isoleucine, DL-phenylalanine and L-histidine monohydrochloride have no effect, at pH 5.0, 35C under shaking conditions at 200 rpm
-
DL-alanine, DL-serine, L-cystine, glycine, L-ornithine monohydrochloride, DL-aspartic acid, L-glutamic acid, DL-valine, L-leucine or L-lysine monohydrochloride significantly induce tannase synthesis at pH 5.0, 35C under shaking conditions at 200 rpm. Maximum tannase production with DL-alanine (2.87fold that of the control). Tannase production with DL-serine, L-ornithine monohydrochloride or L-cystine is 1.67fold, with glycine or DL-valine is 1.7fold, with DL-aspartic acid is 1.89fold, and with L-glutamic acid, L-lysine monohydrochloride or L-leucine is 1.45fold that of the control. Low effect on tannase production with L-proline or DL-tryptophan (1.23fold that of the control)
-
L-cysteine monohydrochloride or DL-threonine are the most potent inhibitors, at pH 5.0, 35C under shaking conditions at 200 rpm. With L-arginine monohydrochloride tannase production is decreased (yield index is 0.78fold)
Bacillus licheniformis KBR6
-
-
DL-methionine, L-tyrosine, L-isoleucine, DL-phenylalanine and L-histidine monohydrochloride have no effect, at pH 5.0, 35C under shaking conditions at 200 rpm
Bacillus licheniformis KBR6
-
-
DL-alanine, DL-serine, L-cystine, glycine, L-ornithine monohydrochloride, DL-aspartic acid, L-glutamic acid, DL-valine, L-leucine or L-lysine monohydrochloride significantly induce tannase synthesis at pH 5.0, 35C under shaking conditions at 200 rpm. Maximum tannase production with DL-alanine (2.87fold that of the control). Tannase production with DL-serine, L-ornithine monohydrochloride or L-cystine is 1.67fold, with glycine or DL-valine is 1.7fold, with DL-aspartic acid is 1.89fold, and with L-glutamic acid, L-lysine monohydrochloride or L-leucine is 1.45fold that of the control. Low effect on tannase production with L-proline or DL-tryptophan (1.23fold that of the control)
Bacillus licheniformis KBR6
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-
in the presence of tannic acid, ATAN1 transcript declines after 12 h of incubation, by 24 h titres of the ATAN1 transcript drop below the detection limit
B7VFD0, -
ATAN1 is expressed only in the presence of tannic acid or gallic acid. Transcripts are first detected 2 h after the shift from glucose to tannic acid medium, levels then increase, reaching a maximum after 4-12 h. ATAN1 transcript is detectable within 30 min in the presence of gallic acid
B7VFD0, -
enzyme production is drastically inhibited at higher concentrations of D-glucose (above 0.5% w/v)
-
intracellular enzyme levels increase 2fold in the presence of 0.75% (w/v) gallic acid, whereas the addition of low concentrations of D-glucose (0.1% w/v) increase both extra- and intracellular activities
-
enzyme production is depleted at higher tannic acid concentrations
Hyalopus sp.
-
organism in liquid submerged fermentation produces maximum extracellular tannase at the end of its exponential phase after 120 h. Wheat bran supports tannase production. 2.5% tannic acid is most suitable for maximum tannase synthesis through solid state fermentation
Hyalopus sp.
-
enzyme production is depleted at higher tannic acid concentrations
Hyalopus sp. DSF3
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-
organism in liquid submerged fermentation produces maximum extracellular tannase at the end of its exponential phase after 120 h. Wheat bran supports tannase production. 2.5% tannic acid is most suitable for maximum tannase synthesis through solid state fermentation
Hyalopus sp. DSF3
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-
tannase production is inducible in the presence of tannic acid. Tannase production is supported to various extents by galactose, maltose, sucrose, dextran and xylitol in the presence of 1.5% tannic acid. 2.0% (w/v) galactose increases tannase production by 1.4fold. Increasing the concentration of ammonium chloride to 0.5% (w/v) significantly increases tannase
-
Lenzites elegans reaches the highest tannase activity at 13 days of growth in media supplemented with glucose (1% w/v), tannic acid (0.5% w/v), and Fabiana densa powder (5% w/v)
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
tannase production by large scale solid-state fermentation optimally on wheat bran with 5% tannic acid producing soluble enzyme and gallic acid during 72 h, enzyme activity on different substrate for solid-state fermentation, overview
additional information
Aspergillus aculeatus DBF9
-
tannase production by large scale solid-state fermentation optimally on wheat bran with 5% tannic acid producing soluble enzyme and gallic acid during 72 h, enzyme activity on different substrate for solid-state fermentation, overview
-
additional information
-
optimization of enzyme production in strain DSB66, (NH4)2HPO4 as nitrogen source results in high enzyme production rates, overview
additional information
Aureobasidium pullulans DBS66
-
optimization of enzyme production in strain DSB66, (NH4)2HPO4 as nitrogen source results in high enzyme production rates, overview
-
additional information
-
active cells of strain KBR6 are immobilized in calcium-alginate and used for the production of tannase, the enzyme production rate is 1.7fold higher than that obtained by free cells, the highest activity is achieved at the third repeated cycle, ten cycles are possible without significant loss of activity
additional information
Bacillus licheniformis KBR6
-
active cells of strain KBR6 are immobilized in calcium-alginate and used for the production of tannase, the enzyme production rate is 1.7fold higher than that obtained by free cells, the highest activity is achieved at the third repeated cycle, ten cycles are possible without significant loss of activity
-
additional information
Penicillium variabile
-
the enzyme immobilized on Amberlite IR retains about 85% of the initial catalytic activity even after ninth cycle of its use, immobilization method optimization, overview
additional information
Penicillium variabile IARI 2031
-
the enzyme immobilized on Amberlite IR retains about 85% of the initial catalytic activity even after ninth cycle of its use, immobilization method optimization, overview
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nutrition
-
the enzyme has wide applications in food, beverage, brewing, cosmetic, and chemical industry, overview
synthesis
-
the enzyme has wide applications in food, beverage, brewing, cosmetic, and chemical industry, overview
nutrition
Aspergillus aculeatus DBF 9
-
the enzyme has wide applications in food, beverage, brewing, cosmetic, and chemical industry, overview
-
synthesis
Aspergillus aculeatus DBF 9
-
the enzyme has wide applications in food, beverage, brewing, cosmetic, and chemical industry, overview
-
food industry
-
tannase is a potential agent for the manufacture of instant tea (tea cream solubilisation)
food industry
Aspergillus awamori BTMFW032
-
tannase is a potential agent for the manufacture of instant tea (tea cream solubilisation)
-
biotechnology
-
production of the enzyme for industrial purposes
agriculture
-
the enzyme is a food processing enzyme used in food, brewing, and feed industry
brewing
-
the enzyme is a food processing enzyme used in food, brewing, and feed industry
food industry
-
the enzyme is a food processing enzyme used in food, brewing, and feed industry
biotechnology
-
production of the enzyme for industrial purposes
biotechnology
-
immobilization of enzyme by microencapsulation with a coacervate calcium alginate membrane surrounding a liquid core. Yield is 36.8% of initial enzyme activity, pH stability and thermal stability improve after microencapsulation. Enzyme can be used for up to 15 runs; immobilization of the enzyme by microencapsulation with a coacervate calcium alginate membrane surrounding a liquid core improves the thermal and pH stability significantly
biotechnology
-
production of the enzyme for industrial purposes, usage in quality improvement in the production of beer, wine
biotechnology
-
production of enzyme by Aspergillus growing on fourfold diluted olive mill waste water is stable during more than 30 h and correlates with about 70% degradation of phenolic compounds present in the waste
food industry
-
the enzyme is used in food and beverage processing, and some of the major commercial applications are the preparation of instant tea, acorn liquor and production of gallic acid
nutrition
-
the enzyme has potential use in the food industry, for example for clarification of beer and fruit juices. Due to the extracellular nature and the high pH and temperature stability of the tannase, the production of the enzyme in the solid-state fermentation has a high potential of economic production, in comparison to a submerged fermentation
synthesis
-
synthesis of gallic esters from gallic acid and alcohols in organic solvents using enzyme microencapsulated with chitosan-alginate complex coacervate membrane. Highest yield is 44.3% in benzene, and 35.7% in hexane, best substrates are 1-propanol, 1-butanol, or 1-pentanol
synthesis
-
the mycelium-bound enzyme is useful as biocatalyst in a whole cell system at proper conditions to higher conversion of propyl gallate, the method could also reduce the cost and the time for the immobilization process
synthesis
-
production of propyl gallate for the food industry and trimethoprim in the pharmaceutical industry
biotechnology
Aspergillus niger HA37
-
production of enzyme by Aspergillus growing on fourfold diluted olive mill waste water is stable during more than 30 h and correlates with about 70% degradation of phenolic compounds present in the waste
-
nutrition
Aspergillus niger PKL 104
-
the enzyme has potential use in the food industry, for example for clarification of beer and fruit juices. Due to the extracellular nature and the high pH and temperature stability of the tannase, the production of the enzyme in the solid-state fermentation has a high potential of economic production, in comparison to a submerged fermentation
-
synthesis
Aspergillus niger PKL 104
-
production of propyl gallate for the food industry and trimethoprim in the pharmaceutical industry
-
biotechnology
-
production of the enzyme for industrial purposes
biotechnology
-
synthesis of enzyme in fed-batch culture, at pH 5.0, achieves 7000 IU/l
biotechnology
-
synthesis both of ellagic acid and enzyme is maximal between 48 h and 72 h of growth of microorganism, at around 28 to 35C and at about 5 g/l tannin
biotechnology
Aspergillus sp. SHL 6
-
synthesis both of ellagic acid and enzyme is maximal between 48 h and 72 h of growth of microorganism, at around 28 to 35C and at about 5 g/l tannin
-
nutrition
-
the enzyme is used in production of instant tea, wine, and gallic acid
nutrition
Bacillus licheniformis KBR 6
-
the enzyme is used in production of instant tea, wine, and gallic acid
-
synthesis
Bacillus licheniformis KBR 6
-
gallate is used for synthesis of propyl gallate, a widely used food antioxidant
-
food industry
Bacillus licheniformis KBR6
-
the enzyme is found to be useful in the manufacture of instant tea, acron wine, coffee-flavoured soft drinks, clarification of beer and fruit juices
-
food industry
-
fruit juice debittering
biotechnology
-
production of the enzyme for industrial purposes
industry
Hyalopus sp.
-
in a short period of time the organism produces a large amount of tannase in an agricultural byproduct and cheap substrate like wheat bran, so in future, this organism can be applied for commercial tannase production. Broad range of pH and temperature stability of the enzyme can be exploited in various ways for pollution control in the leather industry and bioprocess industry in future
industry
Hyalopus sp. DSF3
-
in a short period of time the organism produces a large amount of tannase in an agricultural byproduct and cheap substrate like wheat bran, so in future, this organism can be applied for commercial tannase production. Broad range of pH and temperature stability of the enzyme can be exploited in various ways for pollution control in the leather industry and bioprocess industry in future
-
biotechnology
-
production of the enzyme for industrial purposes
food industry
-
the enzyme is useful in the food-processing industry
food industry
-
the use of Lactobacillus plantarum tannase is an adequate alternative to the fungal tannases currently used in the food industry. Use of tannase may provide an efficient means for obtaining molecules with valuable activities from the degradation of complex tannins present in food and agricultural wastes
nutrition
B3Y018
food and beverage processing
food industry
Lactobacillus plantarum CECT 748(T)
-
the enzyme is useful in the food-processing industry
-
food industry
Lactobacillus plantarum CECT 748T
-
the use of Lactobacillus plantarum tannase is an adequate alternative to the fungal tannases currently used in the food industry. Use of tannase may provide an efficient means for obtaining molecules with valuable activities from the degradation of complex tannins present in food and agricultural wastes
-
biotechnology
-
maximum production of enzyme by growth on coffee husk, supplemented with 0.6% tannic acid, and 50% w/v moisture
biotechnology
Lactobacillus sp. ASR-S1
-
maximum production of enzyme by growth on coffee husk, supplemented with 0.6% tannic acid, and 50% w/v moisture
-
biotechnology
-
production of the enzyme for industrial purposes
biotechnology
-
hydrolysis of tannic acid by enzyme immobilized on alginate beads, enzyme retains about 85% of initial activity and is active after extensive reuse
food industry
-
the enzyme could find potential use in the food-processing industry
food industry
-
the enzyme could be used in the food processing industry
synthesis
Penicillium variabile
-
the enzyme immobilized on Amberlite IR retains about 85% of the initial catalytic activity even after ninth cycle of its use, immobilization method optimization, overview
synthesis
Penicillium variabile IARI 2031
-
the enzyme immobilized on Amberlite IR retains about 85% of the initial catalytic activity even after ninth cycle of its use, immobilization method optimization, overview
-
biotechnology
-
production of the enzyme for industrial purposes
food industry
Rhizopus sp.
-
the enzyme is used in food and beverage processing, and some of the major commercial applications are the preparation of instant tea, acorn liquor and production of gallic acid
food industry
Rhizopus sp. C3-I
-
the enzyme is used in food and beverage processing, and some of the major commercial applications are the preparation of instant tea, acorn liquor and production of gallic acid
-
medicine
-
tanA detection via PCR is a useful method for the rapid and simple identification of Staphylococcus lugdunensis. Detection efficiency of tanA from feces is identical to that from pure culture. The tanA gene can be used as a standard identification marker. The high specificity allows for tanA to be used as an Staphylococcus lugdunensis identification marker in other assays, including DNA microarrays
food industry
-
the enzyme is found to be useful in the manufacture of instant tea, acron wine, coffee-flavoured soft drinks, clarification of beer and fruit juices
additional information
-
sensitive probe for determining the structure of naturally occurring gallic acid esters
synthesis
-
gallate is used for synthesis of propyl gallate, a widely used food antioxidant
additional information
Bacillus licheniformis KBR 6
-
sensitive probe for determining the structure of naturally occurring gallic acid esters
-