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Literature summary for 3.1.1.20 extracted from

  • Flores-Maltos, A.; Rodriguez-Duran, L.V.; Renovato, J.; Contreras, J.C.; Rodriguez, R.; Aguilar, C.N.
    Catalytical properties of free and immobilized Aspergillus niger tannase (2011), Enzyme Res., 2011, 768183.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.4
-
Tannic acid free enzyme, in citrate buffer (50 mM, pH 5.5), at 30°C Aspergillus niger
0.433
-
methyl gallate free enzyme, in citrate buffer (50 mM, pH 5.5), at 30°C Aspergillus niger
0.529
-
methyl gallate Ca alginate-immobilized enzyme, in citrate buffer (50 mM, pH 5.5), at 30°C Aspergillus niger
23.75
-
Tannic acid Ca alginate-immobilized enzyme, in citrate buffer (50 mM, pH 5.5), at 30°C Aspergillus niger

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-
Aspergillus niger GH1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial purification by HiTrap G25 gel filtration (5.4fold purification and 5.6fold concentration with a recovery yield higher than 90%) Aspergillus niger

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methyl gallate + H2O
-
Aspergillus niger gallate + methanol
-
?
methyl gallate + H2O
-
Aspergillus niger GH1 gallate + methanol
-
?
tannic acid + H2O
-
Aspergillus niger gallic acid + D-glucose
-
?
tannic acid + H2O
-
Aspergillus niger GH1 gallic acid + D-glucose
-
?