|Content:||100 assays per kit|
|Storage Temperature:|| Short term stability: 2-8oC, |
Long term stability: See individual component labels
|Stability:||> 2 years under recommended storage conditions|
|Limit of Detection:||1.3 mg/L|
|Reaction Time (min):||~ 70 min|
|Application examples:||Fruit juices and other materials.|
|Method recognition:||Novel method|
This product has been discontinued (read more).
The Arabinan test kit is suitable for the measurement and analysis of Arabinan in fruit juice concentrates.
View all of our polysaccharide assay kits.
- Very rapid reaction due to inclusion of galactose mutarotase (patented technology)
- Very cost effective
- All reagents stable for > 2 years after preparation
- Only enzymatic kit available
- Very specific
- Simple format
- Mega-Calc™ software tool is available from our website for hassle-free raw data processing
- Standard included
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.Hide Abstract
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.Hide Abstract
Interactions of arabinan-rich pectic polysaccharides with polyphenols.
Fernandes, P. A., Le Bourvellec, C., Renard, C. M., Wessel, D. F., Cardoso, S. M. & Coimbra, M. A. (2020). Carbohydrate Polymers, 230, 115644.
Given the high prevalence of arabinan side chains in pectic polysaccharides, this work aims to unveil the impact of their structural diversity on pectic polysaccharides-polyphenol interactions. To assess the effect of arabinan branching degree, sugar beet arabinans (branched and debranched) were used and compared to the well-known structure of apple arabinan and other pectic polysaccharides. Furthermore, arabinans contribution to pectic polysaccharides/polyphenol interactions was assessed. The interactions were evaluated using chlorogenic acid, phloridzin and procyanidins (degree of polymerization of 9). Linear arabinans had 8-fold and 2-fold higher retention for chlorogenic acid and phloridzin, respectively, than branched arabinans. This trend was also observed for the interaction of arabinans with procyanidins. However, arabinans with covalently linked polyphenols showed lower interactions. The interactions involved between arabinans and polyphenols explained 1-28 % of the interactions of pectic polysaccharides, allowing us to conclude that the whole polysaccharide structure is more relevant for polyphenol interactions than each part.Hide Abstract
In-vitro prebiotic analysis of microbiota accessible pectic polysaccharides.
Tingirikari, J. M. R. (2019). Current Microbiology, 76(12), 1452-1460.
Pectin is a diverse polysaccharide comprising of polygalacturonic acid, rhamnogalactouronan, and neutral polysaccharides (arabinan and arabinogalactan) as side chains or branches. They are resistant to salivary amylase and gastric juice. In the present study the prebiotic potentials of different pectic derived substrates were performed by using intestinal cultures and measuring the growth, change in pH and short chain fatty acid, (SCFA) production. Arabinan, arabinogalactan, and rhamnogalacturonan were fermented by probiotic bacteria such as Bifidobacterium breve, Bi. longum, Bi. bifidum, and Bacteroides thetaiotaomicron (commensal bacteria). While, polygalacturonic acid was fermented by Ba. fragilis, Ba. thetaiotaomicron, and Ba. uniformis. All the screened bacteria significantly decreased the pH from 7 to 5 (pH difference of ≈ 2), which clearly indicated that the above bacteria produced the enzymes necessary for the digestion of the pectic derived polysaccharides. The SCFA profiles of the above screened bacteria clearly demonstrated the production of lactate, acetate and propionate which are the key metabolites involved in maintaining gut health and prevention of several intestinal diseases. Thus, pectic polysaccharides hold potential application in food industry as prebiotic ingredients or dietary fibers.Hide Abstract
The hydrophobic polysaccharides of apple pomace.
Fernandes, P. A., Silva, A. M., Evtuguin, D. V., Nunes, F. M., Wessel, D. F., Cardoso, S. M. & Coimbra, M. A. (2019). Carbohydrate Polymers, 223, 115132.
In this work, polysaccharides extracted with hot water from apple pomace were isolated by C18 cartridge solid-phase extraction at pH 7 (Fr7). Dialysis (12-14 kDa) of this fraction allowed to obtain 17% (w/w) of polymeric material composed by 65% of polysaccharides, mainly arabinose (58 mol%), galacturonic acid (16 mol%) and glucose (10 mol%). Folin-Ciocalteu assay showed 62 g of phloridzin equiv/kg of polyphenols. Moreover, adjusting to pH 3, it was possible to retain an additional fraction (Fr3) representing a further 4% of the polymeric material. Fr3 contained 53% of polysaccharides composed mainly by galacturonic acid (66 mol%) and polyphenols accounted for 37 g of phloridzin equiv/kg. Precipitation with ethanol and subsequent methylation and NMR spectroscopic analysis of Fr7 dialysate allowed the identification of covalently-linked pectic-polyphenol-xyloglucan and arabinan-polyphenol complexes. These structures are possibly formed as a result of polyphenol oxidation reactions during the industrial processing of apples, conferring hydrophobic characteristics to apple pomace polysaccharides.Hide Abstract
Kinetics and regioselectivity of three GH62 α-L-arabinofuranosidases from plant pathogenic fungi.
Sarch, C., Suzuki, H., Master, E. R. & Wang, W. (2019). Biochimica et Biophysica Acta (BBA)-General Subjects, 1863(6), 1070-1078.
Backgound: Xylan is the second most abundant plant cell wall polysaccharide after cellulose with α-L-arabinofuranose (L-Araf) as one of the major side substituents. Capacity to degrade xylan is characteristic of many plant pathogens; and corresponding enzymes that debranch arabinoxylan provide tools to tailor xylan functionality or permit its full hydrolysis. Method: Three GH62_2 family α-arabinofuranosidases (Abfs) from plant pathogenic fungi, NhaAbf62A from Nectria haematococca, SreAbf62A from Sporisorium reilianum and GzeAbf62A from Gibberella zeae, were recombinantly produced in Escherichia coli. Their biochemical properties and substrate specificities were characterized in detail. Particularly with 1H NMR, the regioselectivity and debranching preference of the three Abfs were directly compared. Results: The activities of selected Abfs towards arabinoxylan were all optimal at pH 6.5. Their preferred substrates were wheat arabinoxylan, followed by soluble oat spelt xylan. The Abfs displayed selectivity towards either α-(1 → 2) or α-(1 → 3)-L-Araf mono-substituents in arabinoxylan. Specifically, SreAbf62A and GzeAbf62A removed m-α-(1 → 3)-L-Araf and m-α-(1 → 2)-L-Araf substituents with a similar rates, whereas NhaAbf62A released m-α-(1→ 3)-L-Araf 1.9 times faster than m-α-(1 → 2)-L-Araf. Major conclusions: Building upon the known selectivity of GH62 family α-arabinofuranosidases towards L-Araf mono-substituents in xylans, the current study uncovers enzyme-dependent preferences towards m-α-(1 → 3)-L-Araf and m-α-(1 → 2)-L-Araf substitutions. Comparative sequence-structure analyses of Abfs identified an arginine residue in the xylose binding +2R subsite that was correlated to the observed enzyme-dependent L-Araf debranching preferences. General significance: This study expands the limited pool of characterized GH62 Abfs particularly those from plant pathogenic fungi, and provides biochemical details and methodology to evaluate regioselectivity within this glycoside hydrolase family.Hide Abstract
A novel thermostable GH10 xylanase with activities on a wide variety of cellulosic substrates from a xylanolytic Bacillus strain exhibiting significant synergy with commercial Celluclast 1.5 L in pretreated corn stover hydrolysis.
Wang, K., Cao, R., Wang, M., Lin, Q., Zhan, R., Xu, H. & Wang, S. (2019). Biotechnology for Biofuels, 12(1), 48.
Background: Cellulose and hemicellulose are the two largest components in lignocellulosic biomass. Enzymes with activities towards cellulose and xylan have attracted great interest in the bioconversion of lignocellulosic biomass, since they have potential in improving the hydrolytic performance and reducing the enzyme costs. Exploring glycoside hydrolases (GHs) with good thermostability and activities on xylan and cellulose would be beneficial to the industrial production of biofuels and bio-based chemicals. Results: A novel GH10 enzyme (XynA) identified from a xylanolytic strain Bacillus sp. KW1 was cloned and expressed. Its optimal pH and temperature were determined to be pH 6.0 and 65°C. Stability analyses revealed that XynA was stable over a broad pH range (pH 6.0-11.0) after being incubated at 25°C for 24 h. Moreover, XynA retained over 95% activity after heat treatment at 60°C for 60 h, and its half-lives at 65°C and 70°C were about 12 h and 1.5 h, respectively. More importantly, in terms of substrate specificity, XynA exhibits hydrolytic activities towards xylans, microcrystalline cellulose (filter paper and Avicel), carboxymethyl cellulose (CMC), cellobiose, p-nitrophenyl-β-D-cellobioside (pNPC), and p-nitrophenyl-β-D-glucopyranoside (pNPG). Furthermore, the addition of XynA into commercial cellulase in the hydrolysis of pretreated corn stover resulted in remarkable increases (the relative increases may up to 90%) in the release of reducing sugars. Finally, it is worth mentioning that XynA only shows high amino acid sequence identity (88%) with rXynAHJ14, a GH10 xylanase with no activity on CMC. The similarities with other characterized GH10 enzymes, including xylanases and bifunctional xylanase/cellulase enzymes, are no more than 30%. Conclusions: XynA is a novel thermostable GH10 xylanase with a wide substrate spectrum. It displays good stability in a broad range of pH and high temperatures, and exhibits activities towards xylans and a wide variety of cellulosic substrates, which are not found in other GH10 enzymes. The enzyme also has high capacity in saccharification of pretreated corn stover. These characteristics make XynA a good candidate not only for assisting cellulase in lignocellulosic biomass hydrolysis, but also for the research on structure-function relationship of bifunctional xylanase/cellulase.Hide Abstract
Function of a laminin_G_3 module as a carbohydrate‐binding module in an arabinofuranosidase from Ruminiclostridium josui.
Sakka, M., Kunitake, E., Kimura, T. & Sakka, K. (2019). FEBS Letters, 593(1), 42-51.
Laminin_G_3 modules can exist together with family‐43 catalytic modules of glycoside hydrolase (GH43), but their functions are unknown. Here, a laminin_G_3 module and a GH43 module derived from a Ruminiclostridium josui modular arabinofuranosidase Abf43A‐Abf43B‐Abf43C were produced individually as RjLG3 and RjGH43_22, respectively, or combined as RjGH43‐1 to gain insights into their activities. Isothermal calorimetry analysis showed that RjLG3 has high affinity toward 32-α‐L‐arabinofuranosyl‐(1,5)‐α‐L‐arabinotriose but not for α‐1,5‐linked arabinooligosaccharides, which suggests that RjLG3 interacts specifically with a branched arabinofuranosyl residue of an arabinooligosaccharide but not an arabinofuranosyl residue at the end of α‐1,5‐linked arabinooligosaccharides. RjGH43‐1 (with CBM) shows higher activity toward sugar beet arabinan than RjGH43_22 (without CBM), which suggests that the LG3 module in RjGH43‐1 plays an important role in substrate hydrolysis as a carbohydrate‐binding module.Hide Abstract
Functional characterization and comparative analysis of two heterologous endoglucanases from diverging subfamilies of glycosyl hydrolase family 45.
Berto, G. L., Velasco, J., Ribeiro, C. T. C., Zanphorlin, L. M., Domingues, M. N., Murakami, M. T., Polikarpoy, I., Oliveira, L. C., Ferraz, A. & Segato, F. (2019). Enzyme and Microbial Technology, 120, 23-35.
Lignocellulosic materials are abundant, renewable and are emerging as valuable substrates for many industrial applications such as the production of second-generation biofuels, green chemicals and pharmaceuticals. However, the recalcitrance and the complexity of cell wall polysaccharides require multiple enzymes for their complete conversion to oligo- and monosaccharides. The endoglucanases from GH45 family are a small and relatively poorly studied group of enzymes with potential industrial application. The present study reports cloning, heterologous expression and functional characterization of two GH45 endoglucanases from mesophilic fungi Gloeophyllum trabeum (GtGH45) and thermophilic fungi Myceliophthora thermophila (MtGH45), which belong to subfamilies GH45C and GH45A, respectively. Both enzymes have optimal pH 5.0 and melting temperatures (Tm) of 66.0°C and 80.9°C, respectively, as estimated from circular dichroism experiments. The recombinant proteins also exhibited different mode of action when incubated with oligosaccharides ranging from cellotriose to cellohexaose, generating mainly cellobiose and cellotriose (MtGH45) or glucose and cellobiose (GtGH45). The MtGH45 did not show activity against oligosaccharides smaller than cellopentaose while the enzyme GtGH45 was able to depolymerize cellotriose, however with lower efficiency when compared to larger oligosaccharides. Furthermore, both GHs45 were stable up to 70°C for 24 h and useful to enhance initial glucan hydrolysis rates during saccharification of sugarcane pith by a mixture of cellulolytic enzymes. Recombinant GHs45 from diverging subfamilies stand out for differences in substrate specificity appearing as new tools for preparation of enzyme cocktails used in cellulose hydrolysis.Hide Abstract
Degradative enzymes for type II arabinogalactan side chains in Bifidobacterium longum subsp. longum.
Fujita, K., Sakamoto, A., Kaneko, S., Kotake, T., Tsumuraya, Y. & Kitahara, K. (2019). Applied Microbiology and Biotechnology, 103(3), 1299-1310.
Type II arabinogalactan (AG) is a soluble prebiotic fiber stimulating the proliferation of bifidobacteria in the human gut. Larch AG, which is comprised of type II AG, is known to be utilized as an energy source for Bifidobacterium longum subsp. longum (B. longum). We have previously characterized GH43_24 exo-β-1,3-galactanase (Bl1,3Gal) for the degradation of type II AG main chains in B. longum JCM1217. In this study, we characterized GH30_5 exo-β-1,6-galactobiohydrolase (Bl1,6Gal) and GH43_22 α-L-arabinofuranosidase (BlArafA), which are degradative enzymes for type II AG side chains in cooperation with exo-β-1,3-galactanase. The recombinant exo-β-1,6-galactobiohydrolase specifically released β-1,6-galactobiose (β-1,6-Gal2) from the nonreducing terminal of β-1,6-galactooligosaccharides, and the recombinant α-L-arabinofuranosidase released arabinofuranose (Araf) from α-1,3-Araf -substituted β-1,6-galactooligosaccharides. β-1,6-Gal2 was additively released from larch AG by the combined use of type II AG degradative enzymes, including Bl1,3Gal, Bl1,6Gal, and BlArafA. The gene cluster encoding the type II AG degradative enzymes is conserved in all B. longum strains, but not in other bifidobacterial species. The degradative enzymes for type II AG side chains are thought to be important for the acquisition of type II AG in B. longum.Hide Abstract