2-Chloro-4-nitrophenyl-β-(1,3:1,4)-glucotrioside
20 mg
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| Content: | 20 mg |
| Shipping Temperature: | Ambient |
| Storage Temperature: | Below -10oC |
| Physical Form: | Powder |
| Stability: | > 10 years under recommended storage conditions |
| CAS Number: | Not Applicable |
| Synonyms: | 2-Chloro-4-nitrophenyl β-D-glucopyranosyl-(1→4)-β-D-glucopyranosyl-(1→3)-β-D-glucopyranoside |
| Molecular Formula: | C24H34CINO18 |
| Molecular Weight: | 660 |
| Purity: | > 98% |
| Substrate For (Enzyme): | β-Glucanase/Lichenase |
| Assay Format: | Spectrophotometer, Microplate, Auto-analyser |
| Detection Method: | Absorbance |
| Wavelength (nm): | 400-420 |
High purity 2-Chloro-4-nitrophenyl-β-(1,3:1,4)-glucotrioside for use in research, biochemical enzyme assays and in vitro diagnostic analysis. This is a colourimetric substrate for the measurement of lichenase or mixed linkage β-glucanase (endo-1,3:1,4-β-D-glucanase) activity. As this substrate can also be hydrolysed by exo-acting β-glucanase/β-glucosidase enzymes, it is recommended only for the assay of pure enzyme solutions. The corresponding data sheet describes suitable assay conditions.
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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.
Hide Abstract| Symbol : | Not Applicable |
| Signal Word : | Not Applicable |
| Hazard Statements : | Not Applicable |
| Precautionary Statements : | Not Applicable |
