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Literature summary for 3.1.1.20 extracted from
- Tannase sequence from a xerophilic Aspergillus niger strain and production of the enzyme in Pichia pastoris (2015), Mol. Biotechnol., 57, 439-447 .
Application
| Application | Comment | Organism |
|---|---|---|
| additional information | tannases are used in food industries during instant tea manufacture, wine and fruit juice clarification, and for the antinutritional reduction effects of tannins in animal feed. In addition, the enzyme reaction product gallic acid is used for propyl gallate and trimethropim synthesis. Propyl gallate is used as an antioxidant in fats, oils, and beverages, while trimethropim is an important antibacterial drug | Aspergillus niger |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| DNA and amino acid sequence determination nand analysis, sequence comparisons and phylogenetic tree, recombinant expression in Pichia pastoris strain KM71 of the tannase, without the signal sequence, but with secretion signal sequence of Saccharomyces cerevisiae instead of the original signal sequence, the enzyme is secreted | Aspergillus niger |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Aspergillus niger | |
| 0.18 | - |
Tannic acid | recombinant enzyme, pH 5.0, 30°C | Aspergillus niger |  |
| 1.98 | - |
Tannic acid | recombinant enzyme, pH 5.0, 20°C | Aspergillus niger | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Aspergillus niger | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| tannic acid + H2O | Aspergillus niger | - |
gallic acid + ? | - |
? | |
| tannic acid + H2O | Aspergillus niger GH1 | - |
gallic acid + ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus niger | A0A0G3ZA16 | a xerophilic strain isolated from the Mexican semi-desert | - |
| Aspergillus niger GH1 | A0A0G3ZA16 | a xerophilic strain isolated from the Mexican semi-desert | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | the enzyme is highly N-glycosylated, sequence analysis, deglycosylation by endo Hf. The amino acid sequence of strain GH1 tannase has eleven potential N-glycosylation sites: 19NGTL, 54NVTV, 130NGSI, 237NATI, 265NLTS, 280NYTS, 304NGSV, 383NVTY, 451NTTY, 508NATV, and 535NSSF | Aspergillus niger |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant extracellular enzyme from Pichia pastoris strain KM71 culture supernatant by anion exchange chromatography | Aspergillus niger |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 50 | - |
purified recombinant enzyme, pH 5.0, 30°C | Aspergillus niger |
Storage Stability
| Storage Stability | Organism |
|---|---|
| the stability assays follow zero order kinetics with a reaction rate of 0.01 and 0.48%/h at 4 and 30°C, respectively, decreasing to 98.9 and 44.0 % after 120 h | Aspergillus niger |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| methyl gallate + H2O | - |
Aspergillus niger | methanol + gallic acid | - |
? | |
| methyl gallate + H2O | - |
Aspergillus niger GH1 | methanol + gallic acid | - |
? | |
| additional information | tannase activity is measured by gallic acid-rhodanine chromogen formation using gallic acid methyl ester as substrate | Aspergillus niger | ? | - |
? | |
| additional information | tannase activity is measured by gallic acid-rhodanine chromogen formation using gallic acid methyl ester as substrate | Aspergillus niger GH1 | ? | - |
? | |
| tannic acid + H2O | - |
Aspergillus niger | gallic acid + ? | - |
? | |
| tannic acid + H2O | - |
Aspergillus niger GH1 | gallic acid + ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the enzyme contains two structural domains, one with an alpha/beta-hydrolase fold and one lid domain that covers the catalytic site, likely being residues Ser196, Asp448, and His494 the putative catalytic triad, which are connected by a disulfide bond between the neighboring cysteines, Cys195 and Cys495 | Aspergillus niger |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| tannin acyl hydrolase | - |
Aspergillus niger |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | - |
recombinant enzyme | Aspergillus niger |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | 50 | recombinant enzyme, over 40% of maximal activity wihtin this range, optimum temperature at 20°C | Aspergillus niger |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
recombinant enzyme | Aspergillus niger |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 5 | recombinant enzyme, over 80% of maximal activity within this range | Aspergillus niger |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | tannin acyl hydrolases, or tannases, catalyze the hydrolysis of ester bonds in gallotannins, complex tannins, and gallic acid esters, usually with gallic acid as the main product | Aspergillus niger |
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