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|Content:||30 mg or 50 mg|
|Storage Temperature:||Ambient or Below -10oC|
|Stability:||> 10 years under recommended storage conditions|
|Substrate For (Enzyme):||endo-1,4-β-Xylanase, α-Arabinofuranosidase|
High purity 23,33-di-α-L-arabinofuranosyl-xylotriose (A2,3XX) for use in research, biochemical enzyme assays and in vitro diagnostic analysis. It can be used as an analytical standard or as a substrate to help characterise the activities of arabinoxylan degrading enzymes including endo-xylanase, β-xylosidase and α-L-arabinofuranosidase. This compound was prepared by the controlled enzymatic hydrolysis of wheat arabinoxylan.
Data booklets for each pack size are located in the Documents tab.
(Bacteroides ovatus) E-ABFBO21 - α-L-Arabinofuranosidase B21
(Bacteroides ovatus) E-ABFBO25 - α-L-Arabinofuranosidase B25
(Bacteroides ovatus) E-AFASE - α-L-Arabinofuranosidase (Aspergillus niger) E-AFAM2 - α-L-Arabinofuranosidase
(Bifidobacterium adolescentis) E-ABFCJ - α-L-Arabinofuranosidase (Cellvibrio japonicus) E-ABFCT - α-L-Arabinofuranosidase
(Clostridium thermocellum) E-ABFUM - α-L-Arabinofuranosidase (Ustilago maydis) E-XYTR1 - endo-1,4-β-Xylanase M1 (Trichoderma viride) E-XYTR3 - endo-1,4-β-Xylanase M3
(Trichoderma longibrachiatum) E-XYLAA - endo-1,4-β-Xylanase (Aspergillus aculeatus) E-XYAN4 - endo-1,4-β-Xylanase M4 (Aspergillus niger) E-XYRU6 - endo-1,4-β-Xylanase (rumen microorganism) E-XYNAP - endo-1,4-β-Xylanase (Aeromonas punctata) E-XYNBS - endo-1,4-β-Xylanase
(Bacillus stearothermophilus T6) E-XYNACJ - endo-1,4-β-Xylanase (Cellvibrio japonicus) E-XYNBCM - endo-1,4-β-Xylanase (Cellvibrio mixtus) E-XYLNP - endo-1,4-β-Xylanase (Neocallimastix patriciarum) E-XYLATM - endo-1,4-β-Xylanase (Thermotoga maritima) E-BXSEBP - β-Xylosidase (Bacillus pumilus) E-BXSR-1KU - β-D-Xylosidase (Selenomonas ruminantium)
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.
Simultaneous determination of cereal monosaccharides, xylo-and arabinoxylo-oligosaccharides and uronic acids using HPAEC-PAD.
Alyassin, M., Campbell, G. M., O'Neill, H. M. & Bedford, M. R. (2020). Food Chemistry, 315, 126221.
Xylo- and arabinoxylo-oligosaccharides (XOS and AXOS) are of interest for their prebiotic activity. The production of these oligomers might be accompanied with monosaccharides. The measurement of both oligosaccharides and monosaccharides usually requires two methods. The current work presents an HPAEC-PAD method based on gradient elution of aqueous solvents sodium hydroxide and sodium acetate, in contrast to conventional isocratic elution, for the simultaneous separation of 16 standards of monosaccharides, xylo-oligosaccharides, arabinoxylo-oligosaccharides and uronic acids using CarboPac PA 200 column. The presented method showed a stable baseline and high-resolution separation of the standards. The method showed acceptable accuracy and precision. Limits of Detection and Quantitation (LOD and LOQ) were estimated for all the standards. The method was applied to measure the activity of a commercial endoxylanase on wheat bran; a steady release of xylose monosaccharide was observed. Enzyme action on oligosaccharide standards showed a preference for the larger oligosaccharides.Hide Abstract
Insight into the role of α-arabinofuranosidase in biomass hydrolysis: cellulose digestibility and inhibition by xylooligomers.
Xin, D., Chen, X., Wen, P. & Zhang, J. (2019). Biotechnology for Biofuels, 12(1), 64.
Background: α-L-Arabinofuranosidase (ARA), a debranching enzyme that can remove arabinose substituents from arabinoxylan and arabinoxylooligomers (AXOS), promotes the hydrolysis of the arabinoxylan fraction of biomass; however, the impact of ARA on the overall digestibility of cellulose is controversial. In this study, we investigated the effects of the addition of ARA on cellulase hydrolytic action. Results: We found that approximately 15% of the xylan was converted into AXOS during the hydrolysis of aqueous ammonia-pretreated corn stover and that this AXOS fraction was approximately 12% substituted with arabinose. The addition of ARA removes a portion of the arabinose decoration, but the resulting less-substituted AXOS inhibited cellulase action much more effectively; showing an increase of 45.7%. Kinetic experiments revealed that AXOS with a lower degree of arabinose substitution showed stronger affinity for the active site of cellobiohydrolase, which could be the mechanism of increased inhibition. Conclusions: Our findings strongly suggest that the ratio of ARA and other xylanases should be carefully selected to avoid the strong inhibition caused by the less-substituted AXOS during the hydrolysis of arabinoxylan-containing biomass. This study advances our understanding of the inhibitory mechanism of xylooligomers and provides critical new insights into the relationship of ARA addition and cellulose digestibility.Hide Abstract