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Literature summary for 3.2.1.39 extracted from
- Enzymatic Properties of beta-1,3-glucanase from Streptomyces sp. Mo (2013), J. Food Sci., 78, C502-C506.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | the enzyme is secreted | Streptomyces sp. | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 36000 | - |
x * 36000, SDS-PAGE | Streptomyces sp. |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| curdlan + H2O | Streptomyces sp. | the enzyme hydrolyzes selectively curdlan containing only beta-1,3 linkages | laminarioligosaccharides + laminaribiose | hydrolysis of curdlan powder results in the accumulation of laminaribiose | ? |  |
| curdlan + H2O | Streptomyces sp. Mo | the enzyme hydrolyzes selectively curdlan containing only beta-1,3 linkages | laminarioligosaccharides + laminaribiose | hydrolysis of curdlan powder results in the accumulation of laminaribiose | ? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces sp. | - |
curdlan-hydrolyzing strain Mo is separated from soil | - |
| Streptomyces sp. Mo | - |
curdlan-hydrolyzing strain Mo is separated from soil | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native extracellular enzyme from culture filtrate by ammonium sulfate fractionation, gel filtration, and anion exchange chromatography | Streptomyces sp. |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| curdlan + H2O | the enzyme hydrolyzes selectively curdlan containing only beta-1,3 linkages | Streptomyces sp. | laminarioligosaccharides + laminaribiose | hydrolysis of curdlan powder results in the accumulation of laminaribiose | ? | |
| curdlan + H2O | the enzyme hydrolyzes selectively curdlan containing only beta-1,3 linkages | Streptomyces sp. Mo | laminarioligosaccharides + laminaribiose | hydrolysis of curdlan powder results in the accumulation of laminaribiose | ? | |
| Laminaria digitata laminarin + H2O | contains a small amount of beta-1,6 linkages compared with curdlan | Streptomyces sp. | laminarioligosaccharides | - |
? | |
| Laminaria digitata laminarin + H2O | contains a small amount of beta-1,6 linkages compared with curdlan | Streptomyces sp. Mo | laminarioligosaccharides | - |
? | |
| laminariheptaose + H2O | - |
Streptomyces sp. | laminaripentaose + laminaribiose | - |
? | |
| laminariheptaose + H2O | - |
Streptomyces sp. Mo | laminaripentaose + laminaribiose | - |
? | |
| laminarihexaose + H2O | - |
Streptomyces sp. | laminaritetraose + laminaribiose | - |
? | |
| laminarihexaose + H2O | - |
Streptomyces sp. Mo | laminaritetraose + laminaribiose | - |
? | |
| laminaripentaose + H2O | - |
Streptomyces sp. | laminaritriose + laminaribiose | - |
? | |
| additional information | Eisenia bicyclis laminarin, with a higher amount of beta-1,6-linkages, is no substrate for the enzyme. Trisaccharide is inevitably released from the hydrolysis of laminarioligosaccharides with 5 to 7 degrees of polymerization. Although the enzyme cleaves off disaccharide from tetrasaccharide, the reaction rate is lower than those of laminaripentaose to laminariheptaose. The results indicate that the active site of Mo endo-beta-1,3-glucanase can efficiently recognize glucosyl residue chain of greater than laminaripentaose and hydrolyzes the beta-1,3 linkage between the 3rd and 4th glucosyl residue | Streptomyces sp. | ? | - |
? | |
| additional information | Eisenia bicyclis laminarin, with a higher amount of beta-1,6-linkages, is no substrate for the enzyme. Trisaccharide is inevitably released from the hydrolysis of laminarioligosaccharides with 5 to 7 degrees of polymerization. Although the enzyme cleaves off disaccharide from tetrasaccharide, the reaction rate is lower than those of laminaripentaose to laminariheptaose. The results indicate that the active site of Mo endo-beta-1,3-glucanase can efficiently recognize glucosyl residue chain of greater than laminaripentaose and hydrolyzes the beta-1,3 linkage between the 3rd and 4th glucosyl residue | Streptomyces sp. Mo | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 36000, SDS-PAGE | Streptomyces sp. |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| beta-1,3-glucanase | - |
Streptomyces sp. |
| Mo enzyme | - |
Streptomyces sp. |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
- |
Streptomyces sp. |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
stable up to | Streptomyces sp. |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
- |
Streptomyces sp. |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 8 | stable at | Streptomyces sp. |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the enzyme's N-terminal amino acid sequence is VTPPDISVTN | Streptomyces sp. |
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Release 2023.1 (January 2023)
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