α-L-Arabinofuranosidase (Cellvibrio japonicus)
500 Units on pNP-α-Araf at 40oC
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| Content: | 500 Units on pNP-α-Araf at 40oC |
| Shipping Temperature: | Ambient |
| Storage Temperature: | 2-8oC |
| Formulation: | In 3.2 M ammonium sulphate |
| Physical Form: | Suspension |
| Stability: | > 4 years at 4oC |
| Enzyme Activity: | α-Arabinofuranosidase |
| EC Number: | 3.2.1.55 |
| CAZy Family: | GH51 |
| CAS Number: | 9067-74-7 |
| Synonyms: | non-reducing end alpha-L-arabinofuranosidase; alpha-L-arabinofuranoside non-reducing end alpha-L-arabinofuranosidase |
| Source: | Cellvibrio japonicus |
| Molecular Weight: | 55,700 |
| Concentration: | Supplied at ~ 250 U/mL |
| Expression: | Recombinant from Cellvibrio japonicus |
| Specificity: | Hydrolysis of α-1,2- and α-1,3-linked L-arabinofuranose residues from arabinoxylans and branched arabinans. Hydrolyses α-1,5-linked arabino-oligosaccharides at a much lower rate. |
| Specific Activity: | ~ 12 U/mg (40oC, pH 5.5 on p-nitrophenyl-α-L-arabinofuranoside) |
| Unit Definition: | One Unit of α-L-arabinofuranosidase activity is defined as the amount of enzyme required to release one µmole of p-nitrophenol (pNP) per minute from p-nitrophenyl-α-L-arabinofuranoside (2.5 mM) in sodium acetate buffer (100 mM), pH 5.5 at 40oC. |
| Temperature Optima: | 50oC |
| pH Optima: | 5.5 |
| Application examples: | Applications in carbohydrate and biofuels research. |
High purity recombinant α-L-Arabinofuranosidase (Cellvibrio japonicus) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
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Falck, P., Linares-Pastén, J. A., Karlsson, E. N. & Adlercreutz, P. (2017). Food Chemistry, In Press.
An arabinose specific xylanase from glycoside hydrolase family 5 (GH5) was used to hydrolyse wheat and rye arabinoxylan, and the product profile showed that it produced arabinose substituted oligosaccharides (AXOS) having 2-10 xylose residues in the main chain but no unsubstituted xylooligosaccharides (XOS). Molecular modelling showed that the active site has an open structure and that the hydroxyl groups of all xylose residues in the active site are solvent exposed, indicating that arabinose substituents can be accommodated in the glycone as well as the aglycone subsites. The arabinoxylan hydrolysates obtained with the GH5 enzyme stimulated growth of Bifidobacterium adolescentis but not of Lactobacillus brevis. This arabinoxylanase is thus a good tool for the production of selective prebiotics.
Hide Abstract| Symbol : | GHS08 |
| Signal Word : | Danger |
| Hazard Statements : | H334 |
| Precautionary Statements : | P261, P284, P304+P340, P342+P311, P501 |
