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Literature summary extracted from

  • Karakus, E.; Ozler, A.; Pekyardimci, S.
    Noncovalent immobilization of pectinesterase (Prunus armeniaca L.) onto bentonite (2008), Artif. Cells Blood Substit. Immobil. Biotechnol., 36, 535-550.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.11 0.51
-
Pectin immobilized enzyme, Vmax: 14.6 micromol/min/mg, no difference between free and immobilized enzyme in Km but in Vmax (8.4fold higher value) Prunus armeniaca

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.11 Prunus armeniaca
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.11 pectin + H2O
-
Prunus armeniaca ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.11 pectin methyl esterase
-
Prunus armeniaca
3.1.1.11 PME
-
Prunus armeniaca

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.11 50
-
-
Prunus armeniaca

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.11 additional information
-
immobilization stabilzes the enzyme Prunus armeniaca

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.11 9
-
-
Prunus armeniaca