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Literature summary extracted from

  • Azhari, R.; Szlak, A.M.; Ilan, E.; Sideman, S.; Lotan, N.
    Purification and characterization of endo- and exo-inulinase (1989), Biotechnol. Appl. Biochem., 11, 105-117.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.7 EDTA 0.1 M, 80% loss of activity Aspergillus sp.
3.2.1.7 Mg2+
-
Aspergillus sp.
3.2.1.7 Mn2+
-
Aspergillus sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.7 570
-
inulin
-
Aspergillus sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.7 Fe3+ 25 mM, 20fold activation Aspergillus sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.7 53000
-
gel filtration Aspergillus sp.

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.7 Aspergillus sp.
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.7 inulin + H2O
-
Aspergillus sp. oligofructosides fructose oligomers of various length ?
3.2.1.7 additional information the enzyme also exhibits invertase activity Aspergillus sp. ?
-
?