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Literature summary extracted from
- High level expression and characterization of tannase tan7 using Aspergillus niger SH-2 with low-background endogenous secretory proteins as the host (2018), Protein Expr. Purif., 144, 71-75 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.1.1.20 | food industry | tannin acyl hydrolase catalyzes the hydrolysis of hydrolyzable tannins. It is used in the manufacture of instant tea and in the production of gallic acid | Aspergillus niger |
| 3.1.1.20 | synthesis | tannin acyl hydrolase catalyzes the hydrolysis of hydrolyzable tannins. It is used in the manufacture of instant tea and in the production of gallic acid | Aspergillus niger |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.1.20 | gene tan7, recombinant expression in Aspergillus niger strain Bdel4, the recombinant enzyme is secreted to the culture medium | Aspergillus niger |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.1.20 | Ba2+ | - |
Aspergillus niger |  |
| 3.1.1.20 | Ca2+ | - |
Aspergillus niger | |
| 3.1.1.20 | Cu2+ | - |
Aspergillus niger | |
| 3.1.1.20 | EDTA | - |
Aspergillus niger | |
| 3.1.1.20 | Mg2+ | - |
Aspergillus niger | |
| 3.1.1.20 | Ni2+ | - |
Aspergillus niger | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.1.20 | Co2+ | activates by about 30% | Aspergillus niger | |
| 3.1.1.20 | Mn2+ | activates by about 30% | Aspergillus niger | |
| 3.1.1.20 | additional information | K+, Na+ and Cd2+ do not impact the tannase activity | Aspergillus niger |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.1.20 | Aspergillus niger | A2QIR3 | - |
- |
| 3.1.1.20 | Aspergillus niger CBS 513.88 | A2QIR3 | - |
- |
| 3.1.1.20 | Aspergillus niger FGSC A1513 | A2QIR3 | - |
- |
| 3.1.1.20 | Aspergillus niger SH-2 | A2QIR3 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.1.1.20 | glycoprotein | the recombinant extracellular enzyme is glycosylated, deglycosylation by PNGase F | Aspergillus niger |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.1.1.20 | recombinant extracellular enzyme 1.3fold from Aspergillus niger strain Bdel4 culture medium by desalting gel filtration, and gel filtration | Aspergillus niger |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.20 | 40.7 | - |
purified recombinant extracellular enzyme, pH 7.0, 30°C | Aspergillus niger |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.1.20 | propyl gallate + H2O | enzyme activity detection using a method based on the formation of chromogen between enzyme released gallic acid and rhodanine (2-thio-4-ketothiazolidine) | Aspergillus niger | gallic acid + propanol | - |
? | |
| 3.1.1.20 | propyl gallate + H2O | enzyme activity detection using a method based on the formation of chromogen between enzyme released gallic acid and rhodanine (2-thio-4-ketothiazolidine) | Aspergillus niger SH-2 | gallic acid + propanol | - |
? | |
| 3.1.1.20 | propyl gallate + H2O | enzyme activity detection using a method based on the formation of chromogen between enzyme released gallic acid and rhodanine (2-thio-4-ketothiazolidine) | Aspergillus niger FGSC A1513 | gallic acid + propanol | - |
? | |
| 3.1.1.20 | propyl gallate + H2O | enzyme activity detection using a method based on the formation of chromogen between enzyme released gallic acid and rhodanine (2-thio-4-ketothiazolidine) | Aspergillus niger CBS 513.88 | gallic acid + propanol | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.1.20 | ? | x * 61700, about, sequence calculation, x * 70000-100000, recombinant glycosylated enzyme, SDS-PAGE, x * 60000-70000, recombinant deglycosylated enzyme, SDS-PAGE | Aspergillus niger |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.1.20 | An04g04430 | locus name | Aspergillus niger |
| 3.1.1.20 | tan7 | - |
Aspergillus niger |
| 3.1.1.20 | tannin acyl hydrolase | - |
Aspergillus niger |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.20 | 40 | - |
recombinant enzyme | Aspergillus niger |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.20 | 20 | 50 | activity range, tannase activity increases at 20°C through 40°C and displays maximum at 40°C, at temperatures above 40°C, the tannase activity decreases sharply | Aspergillus niger |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.20 | 7 | - |
recombinant enzyme | Aspergillus niger |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.1.20 | 6 | 7.5 | puriifed recombinant extracellular enzyme, stable in the pH range from pH 6.0-7.5 | Aspergillus niger |
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Release 2023.1 (January 2023)
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