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Non-specific endo-1,3(4)-β-Glucanase
(Clostridium thermocellum)

Product code: E-LICACT
€228.00

5,000 Units

Prices exclude VAT

Available for shipping

Content: 5,000 Units
Shipping Temperature: Ambient
Storage Temperature: Below -10oC
Formulation: In 50% (v/v) glycerol
Physical Form: Solution
Stability: Minimum 1 year at 4oC. Check vial for details.
Enzyme Activity: β-Glucanase/Lichenase
EC Number: 3.2.1.6
CAZy Family: GH16
CAS Number: 62213-14-3
Synonyms: endo-1,3(4)-beta-glucanase; 3(or 4)-beta-D-glucan 3(4)-glucanohydrolase
Source: Clostridium thermocellum
Molecular Weight: 29,300
Concentration: Supplied at ~ 1,250 U/mL
Expression: Recombinant from Clostridium thermocellum
Specificity: endo-hydrolysis of (1,3)- or (1,4)-linkages in β-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolysed is itself substituted at C-3. Substrates include laminarin, lichenin and cereal D-glucans.
Specific Activity: ~ 186 U/mg (40oC, pH 6.5 on barley β-glucan); 
~ 395 U/mg (60oC, pH 6.5 on barley β-glucan);
~ 7.2 U/mg (40oC, pH 6.5 on CM-curdlan)
Unit Definition: One Unit of glucanase activity is defined as the amount of enzyme required to release one µmole of glucose reducing-sugar equivalents per minute from barley β-glucan (5 mg/mL) in sodium phosphate buffer (100 mM), pH 6.5 at 40oC.
Temperature Optima: 60oC
pH Optima: 6.5
Application examples: Applications in carbohydrate and biofuels research and in the food and feeds industries.

High purity recombinant Non-specific endo-1,3(4)-β-Glucanase (Clostridium thermocellum) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

See our complete CAZy enzyme products list.

Documents
Certificate of Analysis
Safety Data Sheet
Booklet
Publications
Megazyme publication
Novel approaches to the automated assay of β-glucanase and lichenase activity.

Mangan, D., Liadova, A., Ivory, R. & McCleary, B. V. (2016). Carbohydrate Research, 435, 162-172.

We report herein the development of a novel assay procedure for the measurement of β-glucanase and lichenase (EC 3.2.1.73) in crude enzyme extracts. Two assay formats based on a) a direct cleavage or b) an enzyme coupled substrate were initially investigated. The ‘direct cleavage’ substrate, namely 4,6-O-benzylidene-2-chloro-4-nitrophenyl-β-31-cellotriosyl-β-glucopyranoside (MBG4), was found to be the more generally applicable reagent. This substrate was fully characterised using a crude malt β-glucanase extract, a bacterial lichenase (Bacillus sp.) and a non-specific endo-1,3(4)-β-glucanase from Clostridium thermocellum (EC 3.2.1.6). Standard curves were derived that allow the assay absorbance response to be directly converted to β-glucanase/lichenase activity on barley β-glucan. The specificity of MBG4 was confirmed by analysing the action of competing glycosyl hydrolases that are typically found in malt on the substrate. Manual and automated assay formats were developed for the analysis of a) β-glucanase in malt flour and b) lichenase enzyme extracts and the repeatability of these assays was fully investigated.

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Safety Information
Symbol : Not Applicable
Signal Word : Not Applicable
Hazard Statements : Not Applicable
Precautionary Statements : Not Applicable
Safety Data Sheet
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