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Literature summary for 4.2.2.10 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]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
-
Aspergillus niger

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

pH Stability

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