|Storage Temperature:||Below -10oC|
|Formulation:||In 50% (v/v) glycerol|
|Stability:||Minimum 1 year at 4oC. Check vial for details.|
|Synonyms:||endo-1,3(4)-beta-glucanase; 3(or 4)-beta-D-glucan 3(4)-glucanohydrolase|
|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.|
~ 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.|
|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.
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 188.8.131.52) 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 184.108.40.206). 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.Hide Abstract