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Literature summary extracted from

  • Silva, T.P.; de Albuquerque, F.S.; Dos Santos, C.W.V.; Franco, M.; Caetano, L.C.; Pereira, H.J.V.
    Production, purification, characterization and application of a new halotolerant and thermostable endoglucanase of Botrytis ricini URM 5627 (2018), Biores. Technol., 270, 263-269 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.4 Ca2+
-
Amphobotrys ricini
3.2.1.4 Cu2+
-
Amphobotrys ricini
3.2.1.4 Fe2+
-
Amphobotrys ricini

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.4 additional information
-
additional information the enzyme has a Km of 0.1299 mg/ml and a Vmax of 0.097 mol/min/ml, Michaelis-Menten kinetic modeling Amphobotrys ricini

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.4 Mg2+ activates Amphobotrys ricini
3.2.1.4 Mn2+ activates Amphobotrys ricini
3.2.1.4 Na+ activates Amphobotrys ricini
3.2.1.4 NaCl the endoglucanase revealed a halotolerant profile since its activity increased proportionally to an increase in NaCl concentration. The maximum activity is reached at 2 M NaCl with a 75% increase in activity Amphobotrys ricini
3.2.1.4 Zn2+ activates Amphobotrys ricini

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.4 Amphobotrys ricini
-
-
-
3.2.1.4 Amphobotrys ricini URM 5627
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.4 native enzyme by ammonium sulfate fractionation and gel filtration Amphobotrys ricini

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.4 mycelium solid fermentation of the fungus Botrytis ricini strain URM 5627 on a resin made of sugarcane bagasse, coconut fibre, and wood powder Amphobotrys ricini
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.4 additional information
-
purified native enzyme, 1289.83 U/ml, pH 5.0, 50°C Amphobotrys ricini
3.2.1.4 57.92
-
purified native enzyme, pH 5.0, 50°C Amphobotrys ricini

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.4 carboxymethyl cellulose + H2O 2% solution Amphobotrys ricini ?
-
?
3.2.1.4 carboxymethyl cellulose + H2O 2% solution Amphobotrys ricini URM 5627 ?
-
?
3.2.1.4 additional information the enzyme is able to hydrolyse sugarcane bagasse, rice husk, and wheat bran, with the highest production of reducers/fermentable sugars within 24 h of saccharification for wheat bran (137.21 mg/g). Saccharification of agroindustrial residues, overview Amphobotrys ricini ?
-
?
3.2.1.4 additional information the enzyme is able to hydrolyse sugarcane bagasse, rice husk, and wheat bran, with the highest production of reducers/fermentable sugars within 24 h of saccharification for wheat bran (137.21 mg/g). Saccharification of agroindustrial residues, overview Amphobotrys ricini URM 5627 ?
-
?

Subunits

EC Number Subunits Comment Organism
3.2.1.4 ? x * 39000, SDS-PAGE Amphobotrys ricini

Synonyms

EC Number Synonyms Comment Organism
3.2.1.4 CMCase
-
Amphobotrys ricini
3.2.1.4 endo-1,4-beta-D-glucanase
-
Amphobotrys ricini
3.2.1.4 endoglucanase
-
Amphobotrys ricini

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.4 50
-
-
Amphobotrys ricini

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.4 39 60 the purified enzyme is stable at 39-60°C and pH 4.0-6.0 for 60 min Amphobotrys ricini

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.4 5
-
-
Amphobotrys ricini

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.4 4 6 the purified enzyme is stable at 39-60°C and pH 4.0-6.0 for 60 min Amphobotrys ricini

General Information

EC Number General Information Comment Organism
3.2.1.4 additional information halotolerant endoglucanase Amphobotrys ricini