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Literature summary for 3.2.1.4 extracted from

  • Boyce, A.; Walsh, G.
    Expression and characterisation of a thermophilic endo-1,4-beta-glucanase from Sulfolobus shibatae of potential industrial application (2018), Mol. Biol. Rep., 45, 2201-2211 .
    View publication on PubMed

Application

Application Comment Organism
industry the thermophilic nature and biochemical properties of the enzyme indicate its potential suitability in industrial applications undertaken at high temperature, such as the production of second-generation bioethanol from lignocellulosic feedstocks and in the brewing industry Saccharolobus shibatae

Cloned(Commentary)

Cloned (Comment) Organism
gene ssgluc, sequence comparisons, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain Rosetta-gami B (DE3), subcloning in Escherichia coli strain DH5alpha Saccharolobus shibatae

Organism

Organism UniProt Comment Textmining
Saccharolobus shibatae A0A1B5G0A1
-
-
Saccharolobus shibatae B12 A0A1B5G0A1
-
-
Saccharolobus shibatae DSM 5389 A0A1B5G0A1
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His-tagged enzyme 2535fold from Escherichia coli by nickel affinity chromatography and ultrafiltration Saccharolobus shibatae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
428
-
purified recombinant His-tagged enzyme, pH 4.0, 95°C, substrate carboxymethyl cellulose Saccharolobus shibatae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
barley beta-glucan + H2O best substrate Saccharolobus shibatae ?
-
?
barley beta-glucan + H2O best substrate Saccharolobus shibatae B12 ?
-
?
barley beta-glucan + H2O best substrate Saccharolobus shibatae DSM 5389 ?
-
?
carboxymethyl cellulose + H2O
-
Saccharolobus shibatae ?
-
?
carboxymethyl cellulose + H2O
-
Saccharolobus shibatae B12 ?
-
?
carboxymethyl cellulose + H2O
-
Saccharolobus shibatae DSM 5389 ?
-
?
lichenan + H2O best substrate Saccharolobus shibatae ?
-
?
lichenan + H2O best substrate Saccharolobus shibatae B12 ?
-
?
lichenan + H2O best substrate Saccharolobus shibatae DSM 5389 ?
-
?
additional information the crude enzyme releases reducing sugars from acid-pretreated straw at 75-85°C Saccharolobus shibatae ?
-
?
additional information the crude enzyme releases reducing sugars from acid-pretreated straw at 75-85°C Saccharolobus shibatae B12 ?
-
?
additional information the crude enzyme releases reducing sugars from acid-pretreated straw at 75-85°C Saccharolobus shibatae DSM 5389 ?
-
?
xylan + H2O
-
Saccharolobus shibatae ?
-
?
xylan + H2O
-
Saccharolobus shibatae B12 ?
-
?
xylan + H2O
-
Saccharolobus shibatae DSM 5389 ?
-
?

Subunits

Subunits Comment Organism
? x * 35128, sequence calculation Saccharolobus shibatae

Synonyms

Synonyms Comment Organism
endo-1,4-B-glucanase UniProt Saccharolobus shibatae
endo-1,4-beta-glucanase
-
Saccharolobus shibatae
endo-beta-glucanase
-
Saccharolobus shibatae
endoglucanase
-
Saccharolobus shibatae
ssgluc
-
Saccharolobus shibatae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
95 100 recombinant enzyme Saccharolobus shibatae

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
75 110 recombinant enzyme, over 20% of maximal activity within this range, 50% at 80°C and 105°C, profile overview Saccharolobus shibatae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
75
-
purified recombinant enzyme, completely stable for 1 h, and 98% activity remaining after 2 h Saccharolobus shibatae
80
-
purified recombinant enzyme, completely stable for 1 h, and 90% activity remaining after 2 h Saccharolobus shibatae
85
-
purified recombinant enzyme, completely stable for 1 h, and 84% activity remaining after 2 h Saccharolobus shibatae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
recombinant enzyme Saccharolobus shibatae

pH Range

pH Minimum pH Maximum Comment Organism
3 5 recombinant enzyme, over 91% of maximal activity within this range, pH profile, overview Saccharolobus shibatae

pI Value

Organism Comment pI Value Maximum pI Value
Saccharolobus shibatae sequence calculation
-
4.98