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α-L-Arabinofuranosidase (Aspergillus niger)

Product code: E-AFASE
€202.00

480 Units on pNP-α-Arabf at 40oC

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Content: 480 Units on pNP-α-Arabf at 40oC
Shipping Temperature: Ambient
Storage Temperature: 2-8oC
Formulation: In 3.2 M ammonium sulphate
Physical Form: Suspension
Stability: > 1 year under recommended storage conditions
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: Aspergillus niger
Molecular Weight: 62,000
Concentration: Supplied at ~ 300 U/mL
Expression: From Aspergillus niger
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: ~ 32 U/mg (40oC, pH 5.5 on p-nitrophenyl-α-L-arabinofuranoside); 
~ 12.6 U/mg (on sugar-beet arabinan); 
~ 1.2 U/mg (on wheat arabinoxylan)
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 (5 mM) in sodium acetate buffer (100 mM), pH 4.0 at 40oC.
Temperature Optima: 40oC
pH Optima: 4
Application examples: Applications in carbohydrate and biofuels research.

High purity α-L-Arabinofuranosidase (Aspergillus niger) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

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Documents
Certificate of Analysis
Safety Data Sheet
FAQs Data Sheet
Publications
Megazyme publication
Hydrolysis of wheat flour arabinoxylan, acid-debranched wheat flour arabinoxylan and arabino-xylo-oligosaccharides by β-xylanase, α-L-arabinofuranosidase and β-xylosidase.

McCleary, B. V., McKie, V. A., Draga, A., Rooney, E., Mangan, D. & Larkin, J. (2015). Carbohydrate Research, 407, 79-96.

A range of α-L-arabinofuranosyl-(1-4)-β-D-xylo-oligosaccharides (AXOS) were produced by hydrolysis of wheat flour arabinoxylan (WAX) and acid debranched arabinoxylan (ADWAX), in the presence and absence of an AXH-d3 α-L-arabinofuranosidase, by several GH10 and GH11 β-xylanases. The structures of the oligosaccharides were characterised by GC-MS and NMR and by hydrolysis by a range of α-L-arabinofuranosidases and β-xylosidase. The AXOS were purified and used to characterise the action patterns of the specific α-L-arabinofuranosidases. These enzymes, in combination with either Cellvibrio mixtus or Neocallimastix patriciarum β -xylanase, were used to produce elevated levels of specific AXOS on hydrolysis of WAX, such as 32-α-L-Araf-(1-4)-β-D-xylobiose (A3X), 23-α-L-Araf-(1-4)-β-D-xylotriose (A2XX), 33-α-L-Araf-(1-4)-β-D-xylotriose (A3XX), 22-α-L-Araf-(1-4)-β-D-xylotriose (XA2X), 32-α-L-Araf (1-4)-β-D-xylotriose (XA3X), 23-α-L-Araf-(1-4)-β-D-xylotetraose (XA2XX), 33-α-L-Araf-(1-4)-β-D-xylotetraose (XA3XX), 23 ,33-di-α-L-Araf-(1-4)-β-D-xylotriose (A2+3XX), 23,33-di-α-L-Araf-(1-4)-β-D-xylotetraose (XA2+3XX), 24,34-di-α-L-Araf-(1-4)-β-D-xylopentaose (XA2+3XXX) and 33,34-di-α-L-Araf-(1-4)-β-D-xylopentaose (XA3A3XX), many of which have not previously been produced in sufficient quantities to allow their use as substrates in further enzymic studies. For A2,3XX, yields of approximately 16% of the starting material (wheat arabinoxylan) have been achieved. Mixtures of the α-L-arabinofuranosidases, with specific action on AXOS, have been combined with β-xylosidase and β-xylanase to obtain an optimal mixture for hydrolysis of arabinoxylan to L-arabinose and D-xylose.

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Megazyme publication
Comparison of endolytic hydrolases that depolymerise 1,4-β-D-mannan, 1,5-α-L-arabinan and 1,4-β-D-galactan.

McCleary, B. V. (1991). “Enzymes in Biomass Conversion”, (M. E. Himmel and G. F. Leatham, Eds.), ACS Symposium Series, 460, Chapter 34, pp. 437-449. American Chemical Society, Washington.

Hydrolysis of mannan-type polysaccharides by β-mannanase is dependent on substitution on and within the main-chain as well as the source of the β-mannanase employed. Characterisation of reaction products can be used to define the sub-site binding requirements of the enzymes as well as the fine-structures of the polysaccharides. Action of endo-arabinanase and endo-galactanase on arabinans and arabinogalactans is described. Specific assays for endo-arabinanase and arabinan (in fruit-juice concentrates) are reported.

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Megazyme publication

Novel and selective substrates for the assay of endo-arabinanase.

McCleary, B. V. (1989). "Gums and Stabilisers for the Food Industry, Vol 5”, (G. O. Phillips, D. J. Wedlock and P. A.Williams, Eds.), IRL Press, pp. 291-298.

Substrates and assay procedures for the measurement of endo-1,5-α-L-arabinanase in crude, technical pectinase preparations have been developed. The method of choice employs carboxymethy1-debranched beet araban as substrateT and rate of hydrolysis is measured using the Nelson-Somogyi reducing-sugar procedure with arabinose as the standard. The substrate is physically and chemically stable in solution, and the assay procedure is simple, reliable and specific. Other assay procedures for the measurement of endo-arabinanase which employ dyed debranched araban substrates, are also briefly described.

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Publication

Cloning of an α-L-Arabinofuranosidase and Characterization of Its Action on Mono-and Di-Substituted Xylopyranosyl Units.

Wong, D. W. & Batt, S. (2022). Advances in Enzyme Research, 10(4), 75-82.

An α-L-arabinofuranosidase (ARF) gene of 1503 bp was synthesized, subcloned into pET26b vector, and expressed in Escherichia coli. The enzyme was purified in active form, and consisted of 500 amino acid residues, corresponding to 55 kD based on SDS-PAGE. The affinity-purified protein was characterized using arabinofuranosyl xylooligosaccharides (AXOS) as substrates. The pH effect was investigated showing an optimum at pH 5.5. XaARF catalyzed the cleavage of arabinose at C3 of the xylopyranosyl unit efficiently if the arabinofuranosyl substitution was at the terminal compared to internal xylose units. The enzyme was able to act on di-substituted xylopyranosyl units with the first cleavage at C3 followed by C2 linkages.

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Publication

A conserved enzyme of smut fungi facilitates cell-to-cell extension in the plant bundle sheath.

Ökmen, B., Jaeger, E., Schilling, L., Finke, N., Klemd, A., Lee, Y. J., Wemhoner, R., Pauly, M., Neumann, U. & Doehlemann, G. (2022). Nature Communications, 13(1), 1-13.

Smut fungi comprise one of the largest groups of fungal plant pathogens causing disease in all cereal crops. They directly penetrate host tissues and establish a biotrophic interaction. To do so, smut fungi secrete a wide range of effector proteins, which suppress plant immunity and modulate cellular functions as well as development of the host, thereby determining the pathogen's lifestyle and virulence potential. The conserved effector Erc1 (enzyme required for cell-to-cell extension) contributes to virulence of the corn smut Ustilago maydis in maize leaves but not on the tassel. Erc1 binds to host cell wall components and displays 1,3-β-glucanase activity, which is required to attenuate β-glucan-induced defense responses. Here we show that Erc1 has a cell type-specific virulence function, being necessary for fungal cell-to-cell extension in the plant bundle sheath and this function is fully conserved in the Erc1 orthologue of the barley pathogen Ustilago hordei.

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Publication

Arabinoxylans and cross-linked arabinoxylans: Fermentation and potential application as matrices for probiotic bacterial encapsulation.

Mendez-Encinas, M. A., Carvajal-Millan, E., Simon, S., White, A. K., Chau, H. K., Yadav, M. P., et al. (2022). Food Hydrocolloids for Health, 2, 100085.

Arabinoxylans (AX) and protease treated AX (AXP) were subjected to enzymatic hydrolysis with endoxylanase and arabinofuranosidase to obtain hydrolyzed AX (HAX) and AXP (HAXP), whose ability to promote Bifidobacterium infantis and Bifidobacterium longum growth was investigated. Further, the effect of cross-linked AX on the growth of bifidobacteria was also explored. Bifidobacteria showed the highest growth on AX and AXP, while HAX and HAXP did not have a significant impact on bacterial growth. The laccase cross-linking of AX stimulated the growth of bifidobacteria, possibly due to its gel-like structure which favored the bacteria-substrate (AX) interaction. The laccase-induced cross-linked AX (AXG) and alginate (SA) were used to prepare encapsulating matrices. The ability of AXG-SA matrices to encapsulate and protect probiotic bacteria (Lactobacillus rhamnosus GG, Streptococcus thermophilus and B. longum) viability under storage conditions was investigated. The AXG matrices presented the highest encapsulation efficiencies (55–77%) for all three strains, when AXG-SA and SA matrices were compared. Significantly higher levels (~7 logs) of L. rhamnosus GG were recovered from AXG and AXG-SA matrices after 28 days of storage under aerobic conditions at 4 °C compared to SA matrices (~4 logs). The results indicated that the incorporation of AX into the matrices played a significant role on the survival of encapsulated bacteria during storage, which could be attributed to the stability of the covalent cross-linked network formed during AX gelation that protected bacterial viability. Thus, the matrices based on AXG could be promising materials to encapsulate and protect probiotic bacteria for targeted-delivery to the colon.

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Publication

Glycoside Hydrolase family 30 harbors fungal subfamilies with distinct polysaccharide specificities.

Li, X., Kouzounis, D., Kabel, M. A., de Vries, R. P. & Dilokpimol, A. (2022). New biotechnology, 67, 32-41.

Efficient bioconversion of agro-industrial side streams requires a wide range of enzyme activities. Glycoside Hydrolase family 30 (GH30) is a diverse family that contains various catalytic functions and has so far been divided into ten subfamilies (GH30_1-10). In this study, a GH30 phylogenetic tree using over 150 amino acid sequences was contructed. The members of GH30 cluster into four subfamilies and eleven candidates from these subfamilies were selected for biochemical characterization. Novel enzyme activities were identified in GH30. GH30_3 enzymes possess β-(1→6)-glucanase activity. GH30_5 targets β-(1→6)-galactan with mainly β-(1→6)-galactobiohydrolase catalytic behavior. β-(1→4)-Xylanolytic enzymes belong to GH30_7 targeting β-(1→4)-xylan with several activities (e.g. xylobiohydrolase, endoxylanase). Additionally, a new fungal subfamily in GH30 was proposed, i.e. GH30_11, which displays β-(1→6)-galactobiohydrolase. This study confirmed that GH30 fungal subfamilies harbor distinct polysaccharide specificity and have high potential for the production of short (non-digestible) di- and oligosaccharides.

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Publication

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.

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Publication

Peyer's patch-immunomodulating glucans from sugar cane enhance protective immunity through stimulation of the hemopoietic system.

Sakai, Y., Sato, M., Funami, Y., Ishiyama, A., Hokari, R., Iwatsuki, M., Nagai, T., Otoguro, K., Yamada, H., Ōmura, S. & Kiyohara, H. (2019). International Journal of Biological Macromolecules, 124, 505-514.

The aim of the present study was chemical clarification of in vitro Peyer's patch-immunomodulating polysaccharides in sugar cane molasses, and evaluation of in vivo modulating activity on immune function of T lymphocytes in Peyer's patches and on microenvironment of hemopoietic system. Five kinds of glucans, comprising of dextranase-sensitive and activity-related d-glucosyl moieties, were purified as in vitro Peyer's patch-immunomodulating polysaccharides from the molasses. Oral administration of a glucan-enriched subfraction induced IL-2 and GM-CSF-producing T lymphocytes in Peyer's patches, resulting in enhancement of IL-6 production in a hemopoietic microenvironment to boost neutrophil numbers in the peripheral blood stream. Oral administration of purified glucan or glucan-enrich sub-fraction of sugar cane reduced the number of Plasmodium berghei- or P. yoelii-infected erythrocytes in a murine infection model, using polysaccharide alone or via co-administration with the antimalarial drug, artesunate. These results suggested that Peyer's patch-immunomodulating glucans enhanced protective immunity through axis of Peyer's patches-hemopoietic system.

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Publication

Structure relationship of non-covalent interactions between phenolic acids and arabinan-rich pectic polysaccharides from rapeseed meal.

Zhu, J., Zhang, D., Tang, H., & Zhao, G. (2018). International Journal of Biological Macromolecules, 120, 2597-2603.

Covalent and non-covalent interactions between polyphenols and polysaccharides produced vital consequences on the sensory and nutritive qualities of the many foods. In the present study, the structure dependence of the non–covalent interactions between phenolic acids (PAs) and an arabinan-rich pectic polysaccharide from rapeseed meal (ARPP) was explored. Native RAPP and its hydrolysates as well as twenty-seven structurally diversified PAs were applied. The interaction was determined as the micrograms of PAs adsorbed by per milligram of polysaccharides (Qe, μg/mg). On one hand, the molecular weight (Mw) of ARPP displayed a significant effect on the Qe of ferulic acid and a highest value (412.28 μg/mg) was obtained for the ARPP hydrolysate having a Mw of 76 kDa. On the other hand, the substituent profile of PAs greatly affected their Qe values onto ARPP, although the results are monomer and substituent specific. Specifically, in terms of Qe, hydroxylation favored the interaction by 35.78% to 271.22%, while methylation and esterification weakened the absorption by 44.78% to 230.71% and 16.48% to 78.68%, respectively. The case of esterification is more complicated that the attachment of -OCH3 at 3-position (-26.14% to -77.04%) is adverse but that at 5-position is highly favorable (156.96% to 190.70%) for the interactions.

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Safety Information
Symbol : Not Applicable
Signal Word : Not Applicable
Hazard Statements : Not Applicable
Precautionary Statements : Not Applicable
Safety Data Sheet
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