Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.132 extracted from

  • Sheng, J.; Ji, X.; Zheng, Y.; Wang, Z.; Sun, M.
    Improvement in the thermostability of chitosanase from Bacillus ehimensis by introducing artificial disulfide bonds (2016), Biotechnol. Lett., 38, 1809-1815 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
A207C/L286C mutant enzyme has a longer half-life at 50°C (from 10.5 to 69.3 min) and a 200% higher catalytic efficiency (Kcat/Km) than that of the wild-type enzyme Paenibacillus ehimensis
G113C/D116C at 50°C the wild-type shows less than 37% of the initial activity after 30 min, mutant enzyme G113C/D116C retains 62.0% of its initial activity Paenibacillus ehimensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.8
-
chitosan 40°C, pH not specified in the publication, mutant enzyme A207C/L286C, calculated as micromol reducing sugar liberated from chitosan Paenibacillus ehimensis
4.9
-
chitosan 40°C, pH not specified in the publication, wild-type enzyme, calculated as micromol reducing sugar liberated from chitosan Paenibacillus ehimensis

Organism

Organism UniProt Comment Textmining
Paenibacillus ehimensis O24825
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
chitosan + H2O
-
Paenibacillus ehimensis ?
-
?

Synonyms

Synonyms Comment Organism
chitosanase EAG1
-
Paenibacillus ehimensis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
30 min, wild-type shows less than 37% of the initial activity, mutant enzyme G113C/D116C retains 62.0% of its initial activity, mutant enzyme A207C//L286C retains 81.0% of its initial activity Paenibacillus ehimensis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5
-
chitosan 40°C, pH not specified in the publication, wild-type enzyme, calculated as micromol reducing sugar liberated from chitosan Paenibacillus ehimensis
4.9
-
chitosan 40°C, pH not specified in the publication, mutant enzyme A207C/L286C, calculated as micromol reducing sugar liberated from chitosan Paenibacillus ehimensis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.52
-
chitosan 40°C, pH not specified in the publication, wild-type enzyme, calculated as micromol reducing sugar liberated from chitosan Paenibacillus ehimensis
1.03
-
chitosan 40°C, pH not specified in the publication, mutant enzyme A207C/L286C, calculated as micromol reducing sugar liberated from chitosan Paenibacillus ehimensis