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Literature summary for 3.2.1.8 extracted from

  • Shei, J.C.; Fratzke, A.R.; Frederick, M.M.; Frederick, J.R.; Reilly, P.J.
    Purification and characterization of endo-xylanases from Aspergillus niger. II. An enzyme of pI 4.5 (1985), Biotechnol. Bioeng., 27, 533-538.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
Cr2+ 7.5 mM, strong inhibition Aspergillus niger
Cu2+ 7.5 mM, strong inhibition Aspergillus niger
Hg2+ 7.5 mM, strong inhibition Aspergillus niger
Mn2+ 7.5 mM, strong inhibition Aspergillus niger

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
16500
-
 gel filtration Aspergillus niger

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Aspergillus niger

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,4-beta-D-xylan + H2O
-
 Aspergillus niger additional information
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Aspergillus niger

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
48
-
 pH 5.5-5.6, half-life: 40 h Aspergillus niger

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.9
-
-
 Aspergillus niger

pH Range

pH Minimum pH Maximum Comment Organism
3.5 6.5 pH 3.5: about 40% of maximal activity, pH 6.5: about 35% of maximal activity Aspergillus niger

pH Stability

pH Stability pH Stability Maximum Comment Organism
5.5 5.6 48°C, 50% loss of activity after 40 h Aspergillus niger