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Literature summary extracted from

  • Kester, H.C.M.; Visser, J.
    Purification and characterization of pectin lyase B, a novel pectinolytic enzyme from Aspergillus niger (1994), FEMS Microbiol. Lett., 120, 63-68.
No PubMed abstract available

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.2.10 additional information
-
 additional information
-
 Aspergillus niger

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.2.10 Ca2+ optimal concentration: 0.04 M CaCl2 Aspergillus niger
4.2.2.10 Na+ optimal concentration: 0.6 M Aspergillus niger

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.2.10 40000
-
 x * 40000, SDS-PAGE Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
4.2.2.10 Aspergillus niger
-
 multicopy pki-pelB fusion transsformant N593(pPK-PLB)6
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.2.10
-
 Aspergillus niger

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.2.10 additional information
-
-
 Aspergillus niger

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.2.10 pectin highly esterified pectin, DE 94.6% Aspergillus niger ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.2.10 ? x * 40000, SDS-PAGE Aspergillus niger

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
4.2.2.10 6
-
 reversible inactivation above Aspergillus niger