300 Units exo-1,3-β-glucanase / 60 Units β-glucosidase
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|Content:||300 Units exo-1,3-β-glucanase / 60 Units β-glucosidase|
|Formulation:||In 3.2 M ammonium sulphate|
|Stability:||Minimum 1 year at 4oC. Check vial for details.|
|Enzyme Activity:||β-Glucosidase, exo-1,3-β-Glucanase|
|CAZy Family:||GH3, GH55|
exo-1,3-β-Glucanase: glucan 1,3-beta-glucosidase; 3-beta-D-glucan glucohydrolase
exo-1,3-β-Glucanase: Trichoderma virens,
β-Glucosidase: Aspergillus niger
|Concentration:||exo-1,3-β-Glucanase (100 U/mL) / β-Glucosidase (20 U/mL)|
exo-1,3-β-D-Glucanase: From Trichoderma sp.
β-Glucosidase: From Aspergillus niger
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.
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.
|Application examples:||For use in the determination of (1,3)(1,4) β-glucan.|
High purity exo-1,3-β-D-Glucanase (Trichoderma sp.) + β-Glucosidase (Aspergillus niger) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
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