exo-1,3-β-D-Glucanase + β-Glucosidase
300 Units exo-1,3-β-glucanase / 60 Units β-glucosidase
| Content: | 300 Units exo-1,3-β-glucanase / 60 Units β-glucosidase |
| Shipping Temperature: | Ambient |
| Storage Temperature: | 2-8oC |
| Formulation: | In 3.2 M ammonium sulphate |
| Physical Form: | Suspension |
| Stability: | > 1 year under recommended storage conditions |
| Enzyme Activity: | β-Glucosidase, exo-1,3-β-Glucanase |
| EC Number: |
exo-1,3-β-glucanase: 3.2.1.58 β-glucosidase: 3.2.1.21 |
| CAZy Family: | GH3, GH55 |
| CAS Number: |
exo-1,3-β-glucanase: 9073-49-8 β-glucosidase: 9001-22-3 |
| Synonyms: |
exo-1,3-β-Glucanase: glucan 1,3-beta-glucosidase; 3-beta-D-glucan glucohydrolase β-Glucosidase: beta-glucosidase |
| Source: |
exo-1,3-β-Glucanase: Trichoderma sp. β-Glucosidase: Aspergillus sp. |
| Concentration: | exo-1,3-β-Glucanase (100 U/mL) / β-Glucosidase (20 U/mL) |
| Expression: |
exo-1,3-β-D-Glucanase: Recombinant from Trichoderma sp. β-Glucosidase: Purified from Aspergillus sp. |
| Specificity: |
exo-1,3-β-glucanase: Successive hydrolysis of β-D-glucose units from the non-reducing ends of (1,3)-β-D-glucans, releasing α-glucose. β-glucosidase: Hydrolysis of terminal, non-reducing β-D-glucosyl residues with release of β-D-glucose. |
| Unit Definition: |
exo-1,3-β-D-Glucanase: One Unit of exo-1,3-β-glucanase activity is defined as the amount of enzyme required to release one µmole of glucose reducing-sugar equivalents per minute from laminarin (10 mg/mL) in sodium acetate buffer (100 mM), pH 4.0 at 40oC. β-Glucosidase: One Unit of β-glucosidase activity is defined as the amount of enzyme required to release one µmole of p-nitrophenol per minute from 4-nitrophenyl-β-D-glucpyranoside in sodium acetate buffer (100 mM), pH 4.0 at 40oC. |
| Temperature Optima: | 40oC |
| pH Optima: | 4 |
| Application examples: | For use in the determination of (1,3)(1,6) β-glucan. |
A change in the formulation of the Exo-1,3-β-D-Glucanase + β-Glucosidase (E-EXBGOS) product has occurred. For full details please review here.
High purity exo-1,3-β-D-Glucanase (Trichoderma sp.) + β-Glucosidase (Aspergillus sp.) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
A wide range of other Carbohydrate Active enZYmes also available.
Rieder, A., Grimmer, S., Aachmann, F. L., Westereng, B., Kolset, S. O. & Knutsen, S. H. (2013). Carbohydrate Polymers, 92(2), 2075-2083.
Even if carbohydrate preparations from plant/fungal sources have a high degree of purity, observed immune-stimulation may be caused by minute sample contaminations. Using the example of different β-glucans we present a range of analytical tools crucial for validation of possible immune-stimulatory effects. Two yeast (MacroGard and Zymosan) and one cereal β-glucan (CBG40) increased IL-8 secretion by HT-29 cells considerably. Degradation of the β-glucan samples with β-glucan specific enzymes did hardly influence the effect of Zymosan and CBG40 but significantly decreased the effect of MacroGard. Stimulation of IL-8 secretion by CBG40 and Zymosan was hence not due to their β-glucan content. Instead, the effect of the CBG40 sample was due to low levels of LPS despite the inability of the known LPS inhibitor Polymyxin B to supress its stimulatory effect. We conclude that targeted enzymatic degradation of samples is a powerful validation tool to investigate carbohydrate specific immune-modulation.
Hide Abstract| Symbol : | Not Applicable |
| Signal Word : | Not Applicable |
| Hazard Statements : | Not Applicable |
| Precautionary Statements : | Not Applicable |
