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Literature summary extracted from
- Characterisation of a novel Bacillus sp. SJ-10 beta-1,3-1,4-glucanase isolated from jeotgal, a traditional Korean fermented fish (2013), Bioprocess Biosyst. Eng., 36, 721-727.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.73 | gene bg1314, DNA and amino acid sequence determination and analysis, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21 | Bacillus sp. (in: Bacteria) |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.2.1.73 | extracellular | - |
Bacillus sp. (in: Bacteria) | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.73 | additional information | the enzyme is halotolerant | Bacillus sp. (in: Bacteria) |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.73 | 26800 | - |
x * 26800, about, sequence calculation | Bacillus sp. (in: Bacteria) |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.73 | beta-1,3-1,4-glucan + H2O | Bacillus sp. (in: Bacteria) | beta-1,3-1,4-glucanase can hydrolyse only the beta-1,4-glycosidic bond adjacent to beta-1,3-glycosidic bond in the mixed glycosidic linkages of beta-glucan, but cannot hydrolyse the beta-1,4-glycosidic bond in cellulose | 3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose | - |
? |  |
| 3.2.1.73 | beta-1,3-1,4-glucan + H2O | Bacillus sp. (in: Bacteria) SJ-10 | beta-1,3-1,4-glucanase can hydrolyse only the beta-1,4-glycosidic bond adjacent to beta-1,3-glycosidic bond in the mixed glycosidic linkages of beta-glucan, but cannot hydrolyse the beta-1,4-glycosidic bond in cellulose | 3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose | - |
? | |
| 3.2.1.73 | additional information | Bacillus sp. (in: Bacteria) | beta-1,3-1,4-glucanase is an endo-beta-glucanase that cleaves the beta-1,4-linkage in the presence of alphabeta-1,3-linkage in mixed-linkage beta-1,3-1,4-glucans | ? | - |
? | |
| 3.2.1.73 | additional information | Bacillus sp. (in: Bacteria) SJ-10 | beta-1,3-1,4-glucanase is an endo-beta-glucanase that cleaves the beta-1,4-linkage in the presence of alphabeta-1,3-linkage in mixed-linkage beta-1,3-1,4-glucans | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.73 | Bacillus sp. (in: Bacteria) | I1W007 | gene bg1314 | - |
| 3.2.1.73 | Bacillus sp. (in: Bacteria) SJ-10 | I1W007 | gene bg1314 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.73 | recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography to homogeneity | Bacillus sp. (in: Bacteria) |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.73 | beta-1,3-1,4-glucan + H2O | beta-1,3-1,4-glucanase can hydrolyse only the beta-1,4-glycosidic bond adjacent to beta-1,3-glycosidic bond in the mixed glycosidic linkages of beta-glucan, but cannot hydrolyse the beta-1,4-glycosidic bond in cellulose | Bacillus sp. (in: Bacteria) | 3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose | - |
? | |
| 3.2.1.73 | beta-1,3-1,4-glucan + H2O | from oat and barley | Bacillus sp. (in: Bacteria) | 3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose | - |
? | |
| 3.2.1.73 | beta-1,3-1,4-glucan + H2O | beta-1,3-1,4-glucanase can hydrolyse only the beta-1,4-glycosidic bond adjacent to beta-1,3-glycosidic bond in the mixed glycosidic linkages of beta-glucan, but cannot hydrolyse the beta-1,4-glycosidic bond in cellulose | Bacillus sp. (in: Bacteria) SJ-10 | 3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose | - |
? | |
| 3.2.1.73 | beta-1,3-1,4-glucan + H2O | from oat and barley | Bacillus sp. (in: Bacteria) SJ-10 | 3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose | - |
? | |
| 3.2.1.73 | lichenan + H2O | - |
Bacillus sp. (in: Bacteria) | ? | - |
? | |
| 3.2.1.73 | lichenan + H2O | - |
Bacillus sp. (in: Bacteria) SJ-10 | ? | - |
? | |
| 3.2.1.73 | additional information | beta-1,3-1,4-glucanase is an endo-beta-glucanase that cleaves the beta-1,4-linkage in the presence of alphabeta-1,3-linkage in mixed-linkage beta-1,3-1,4-glucans | Bacillus sp. (in: Bacteria) | ? | - |
? | |
| 3.2.1.73 | additional information | thin layer product identification | Bacillus sp. (in: Bacteria) | ? | - |
? | |
| 3.2.1.73 | additional information | beta-1,3-1,4-glucanase is an endo-beta-glucanase that cleaves the beta-1,4-linkage in the presence of alphabeta-1,3-linkage in mixed-linkage beta-1,3-1,4-glucans | Bacillus sp. (in: Bacteria) SJ-10 | ? | - |
? | |
| 3.2.1.73 | additional information | thin layer product identification | Bacillus sp. (in: Bacteria) SJ-10 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.73 | ? | x * 26800, about, sequence calculation | Bacillus sp. (in: Bacteria) |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.73 | beta-1,3-1,4-glucanase | - |
Bacillus sp. (in: Bacteria) |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.73 | 50 | - |
- |
Bacillus sp. (in: Bacteria) |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.73 | 10 | 90 | over 50% of maximal activity within this range, profile overview. The enzyme shows 75, 88, 90 and 80% activity at 20, 40, 60 and 80°C, respectively | Bacillus sp. (in: Bacteria) |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.73 | 50 | - |
purified recombinant His-tagged enzyme, pH 6.0, 30 min, completely stable | Bacillus sp. (in: Bacteria) |
| 3.2.1.73 | 65 | - |
purified recombinant His-tagged enzyme, pH 6.0, 30 min, loss of 50% activity | Bacillus sp. (in: Bacteria) |
| 3.2.1.73 | 70 | - |
purified recombinant His-tagged enzyme, pH 6.0, 30 min, inactivation | Bacillus sp. (in: Bacteria) |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.73 | 6 | - |
- |
Bacillus sp. (in: Bacteria) |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.73 | 3 | 11 | over 50% of maximal activity within this range, profile overview | Bacillus sp. (in: Bacteria) |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.73 | 3 | 11 | purified recombinant His-tagged enzyme, 50°C, 30 min, completely stable | Bacillus sp. (in: Bacteria) |
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