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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 analytical testing applications.

A wide range of other Carbohydrate Active enZYmes also available.

Publications

Cover image for publication: Determination of total dietary fibre and available carbohydrates
Generic tools to assess genuine carbohydrate specific effects on in vitro immune modulation exemplified by β-glucans.

Rieder, A., Grimmer, S., Aachmann, F. L., Westereng, B., Kolset, S. O. & Knutsen, S. H. (2013). Carbohydrate Polymers, 92(2), 2075-2083.

Generic tools to assess genuine carbohydrate specific effects on in vitro immune modulation exemplified by β-glucans.

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.

Link to Article

Safety Information

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