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Literature summary extracted from

  • Fuentes-Garibay, J.A.; Aguilar, C.N.; Rodriguez-Herrera, R.; Guerrero-Olazaran, M.; Viader-Salvado, J.M.
    Tannase sequence from a xerophilic Aspergillus niger strain and production of the enzyme in Pichia pastoris (2015), Mol. Biotechnol., 57, 439-447 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.1.20 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)

EC Number Cloned (Comment) Organism
3.1.1.20 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.20 additional information
-
 additional information Michaelis-Menten kinetics Aspergillus niger
3.1.1.20 0.18
-
 Tannic acid recombinant enzyme, pH 5.0, 30°C Aspergillus niger
3.1.1.20 1.98
-
 Tannic acid recombinant enzyme, pH 5.0, 20°C Aspergillus niger

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.20 extracellular
-
 Aspergillus niger
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.20 tannic acid + H2O Aspergillus niger
-
 gallic acid + ?
-
 ?
3.1.1.20 tannic acid + H2O Aspergillus niger GH1
-
 gallic acid + ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.20 Aspergillus niger A0A0G3ZA16 a xerophilic strain isolated from the Mexican semi-desert
-
3.1.1.20 Aspergillus niger GH1 A0A0G3ZA16 a xerophilic strain isolated from the Mexican semi-desert
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.1.20 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)

EC Number Purification (Comment) Organism
3.1.1.20 recombinant extracellular enzyme from Pichia pastoris strain KM71 culture supernatant by anion exchange chromatography 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 50
-
 purified recombinant enzyme, pH 5.0, 30°C Aspergillus niger

Storage Stability

EC Number Storage Stability Organism
3.1.1.20 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.20 methyl gallate + H2O
-
 Aspergillus niger methanol + gallic acid
-
 ?
3.1.1.20 methyl gallate + H2O
-
 Aspergillus niger GH1 methanol + gallic acid
-
 ?
3.1.1.20 additional information tannase activity is measured by gallic acid-rhodanine chromogen formation using gallic acid methyl ester as substrate Aspergillus niger ?
-
 ?
3.1.1.20 additional information tannase activity is measured by gallic acid-rhodanine chromogen formation using gallic acid methyl ester as substrate Aspergillus niger GH1 ?
-
 ?
3.1.1.20 tannic acid + H2O
-
 Aspergillus niger gallic acid + ?
-
 ?
3.1.1.20 tannic acid + H2O
-
 Aspergillus niger GH1 gallic acid + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.20 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

EC Number Synonyms Comment Organism
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 20
-
 recombinant enzyme Aspergillus niger

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.20 10 50 recombinant enzyme, over 40% of maximal activity wihtin this range, optimum temperature at 20°C Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.20 5
-
 recombinant enzyme Aspergillus niger

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.20 4 5 recombinant enzyme, over 80% of maximal activity within this range Aspergillus niger

General Information

EC Number General Information Comment Organism
3.1.1.20 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