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Literature summary for 4.2.2.2 extracted from

  • Dixit, V.S.; Kumar, A.R.; Pant, A.; Khan, M.I.
    Low molecular mass pectate lyase from Fusarium moniliforme: similar modes of chemical and thermal denaturation (2004), Biochem. Biophys. Res. Commun., 315, 477-484.
    View publication on PubMed
Search for more literature for 4.2.2.2

General Stability

General Stability Organism
the enzyme is reversibly unfolded by urea and guanidine-HCl at its optimal pH of 8.5 Fusarium verticillioides

Organism

Organism UniProt Comment Textmining
Fusarium verticillioides
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
thermal denaturation at 75°C for 10 min is reversible. The enzyme is reversibly unfolded by urea and guanidine-HCl at its optimal pH of 8.5 Fusarium verticillioides

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
 10 min, stable Fusarium verticillioides
45
-
 10 min, about 10% loss of activity Fusarium verticillioides
50
-
 10 min, about 35% of maximal activity Fusarium verticillioides
55
-
 10 min, about 80% of maximal activity Fusarium verticillioides
75
-
 10 min, thermal denaturation is reversible Fusarium verticillioides