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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Enzyme synergy for the production of arabinoxylo-oligosaccharides from highly substituted arabinoxylan and evaluation of their prebiotic potential.
Bhattacharya, A., Ruthes, A., Vilaplana, F., Karlsson, E. N., Adlecreutz, P. & Stålbrand, H. (2020). LWT, 131, 109762.
Wheat bran arabinoxylan can be converted by enzymatic hydrolysis into short arabinoxylo-oligosaccharides (AXOS) with prebiotic potential. Alkali extraction of arabinoxylan from wheat-bran offers advantages in terms of yield and results in arabinoxylan with highly-substituted regions which has been a challenge to hydrolyse using endoxylanases. We show that this hurdle can be overcome by selecting an arabinoxylanase that attacks these regions. The yield of AXOS can be increased by enzyme synergy, involving the hydrolysis of some arabinoxylan side groups. Thus, arabinoxylanase (CtXyl5At) from Clostridium thermocellum, belonging to subfamily 34 of glycoside hydrolase (GH) family 5 was investigated pertaining to its specificity for highly-substituted regions in the arabinoxylan-backbone. CtXyl5At preferentially hydrolysed the water-soluble fraction of alkali-extracted arabinoxylan. AXOS with DP 2-4 were determined as major products from CtXyl5At catalyzed hydrolysis. Increase in AXOS yield was observed with enzyme synergy, involving an initial treatment of soluble arabinoxylan with a GH43 α-l-arabinofuranosidase from Bifidobacterium adolescentis termed BaAXHd3 (30°C, 6h), followed by hydrolysis with CtXyl5At (50°C, 24h). The prebiotic potential of AXOS was shown by growth analysis using the human gut bacteria Bifidobacterium adolescentis ATCC 15703 and Roseburia hominis DSM 6839. Importantly, AXOS were utilized by the bacteria and short-chain fatty acids were produced.
Arabinoxylanase from glycoside hydrolase family 5 is a selective enzyme for production of specific arabinoxylooligosaccharides.
Falck, P., Linares-Pastén, J. A., Karlsson, E. N. & Adlercreutz, P. (2017). Food Chemistry, 242, 579-584.
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 |
