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L-Rhamnose Assay Kit

Product code: K-RHAMNOSE
€168.00

50 / 100 assays (manual) / 550 assays (microplate) / 550 assays (auto-analyser)

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Content: 50 / 100 assays (manual) / 550 assays (microplate) / 550 assays (auto-analyser)
Shipping Temperature: Ambient
Storage Temperature: Short term stability: 2-8oC,
Long term stability: See individual component labels
Stability: > 2 years under recommended storage conditions
Analyte: L-Rhamnose
Assay Format: Spectrophotometer, Microplate, Auto-analyser
Detection Method: Absorbance
Wavelength (nm): 340
Signal Response: Increase
Linear Range: 5 to 100 µg of L-rhamnose per assay
Limit of Detection: ~ 1.2 mg/L
Reaction Time (min): ~ 5 min at 25oC or ~ 4 min at 37oC
Application examples: Hydrolysates of plant material and polysaccharides, culture media / supernatants and other materials.
Method recognition: Novel method

The L-Rhamnose Assay Kit for the measurement of L-rhamnose in plant extracts, culture media/supernatants and other materials is a simple, rapid method.

L-Rhamnose occurs naturally in the L-form and is commonly present as a component of the carbohydrate moiety of eukaryotic glycoproteins and in plant cell wall polysaccharides. The most abundant occurrence of L-rhamnose is within the pectic fraction of plant cell wall polysaccharides. L-Rhamnose is commonly used as a non-metabolisable marker along with lactulose for dual-permeability testing in the diagnosis of intestinal diseases such as Crohn’s disease or coeliac disease.

Note for Content: The number of manual tests per kit can be doubled if all volumes are halved.  This can be readily accommodated using the MegaQuantTM  Wave Spectrophotometer (D-MQWAVE).

View more of our monosaccharide and disaccharide assay kits.

Scheme-K-RHAMNOSE RHAMNOSE Megazyme

Advantages
  • Very cost effective 
  • All reagents stable for > 2 years after preparation 
  • Only test kit available 
  • Simple format 
  • Rapid reaction (~ 5 min at 25oC or ~ 4 min at 37oC) 
  • Mega-Calc™ software tool is available from our website for hassle-free raw data processing 
  • Standard included 
  • Suitable for manual, microplate and auto-analyser formats
Documents
Certificate of Analysis
Safety Data Sheet
FAQs Assay Protocol Data Calculator
Publications
Publication

A new, quick, and simple protocol to evaluate microalgae polysaccharide composition.

Decamp, A., Michelo, O., Rabbat, C., Laroche, C., Grizeau, D., Pruvost, J. & Gonçalves, O. (2021). Marine Drugs, 19(2), 101.

In this work, a new methodological approach, relying on the high specificity of enzymes in a complex mixture, was developed to estimate the composition of bioactive polysaccharides produced by microalgae, directly in algal cultures. The objective was to set up a protocol to target oligomers commonly known to be associated with exopolysaccharides’ (EPS) nutraceutical and pharmaceutical activities (i.e., rhamnose, fucose, acidic sugars, etc.) without the constraints classically associated with chromatographic methods, while maintaining a resolution sufficiently high to enable their monitoring in the culture system. Determination of the monosaccharide content required the application of acid hydrolysis (2 M trifluoroacetic acid) followed by NaOH (2 M) neutralization. Quantification was then carried out directly on the fresh hydrolysate using enzyme kits corresponding to the main monosaccharides in a pre-determined composition of the polysaccharides under analysis. Initial results showed that the enzymes were not sensitive to the presence of TFA and NaOH, so the methodology could be carried out on fresh hydrolysate. The limits of quantification of the method were estimated as being in the order of the log of nanograms of monosaccharides per well, thus positioning it among the chromatographic methods in terms of analytical performance. A comparative analysis of the results obtained by the enzymatic method with a reference method (high-performance anion-exchange chromatography) confirmed good recovery rates, thus validating the closeness of the protocol. Finally, analyses of raw culture media were carried out and compared to the results obtained in miliQ water; no differences were observed. The new approach is a quick, functional analysis method allowing routine monitoring of the quality of bioactive polysaccharides in algal cultures grown in photobioreactors.

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Publication

Addition of pectin-alginate to a carbohydrate beverage does not maintain gastrointestinal barrier function during exercise in hot-humid conditions better than carbohydrate ingestion alone.

Flood, T. R., Montanari, S., Wicks, M., Blanchard, J., Sharpe, H., Taylor, L., Kuennen, M. R. & Lee, B. J. (2020). Applied Physiology, Nutrition, and Metabolism, 45(10).

The objective of this study was to compare the effects of consuming a 16% maltodextrin+fructose+pectin-alginate (MAL+FRU+PEC+ALG) drink against a nutrient-matched maltodextrin+fructose (MAL+FRU) drink on enterocyte damage and gastrointestinal permeability after cycling in hot and humid conditions. Fourteen recreational cyclists (7 men) completed 3 experimental trials in a randomized placebo-controlled design. Participants cycled for 90 min (45% maximal aerobic capacity) and completed a 15-min time-trial in hot (32°C) humid (70% relative humidity) conditions. Every 15 min, cyclists consumed 143 mL of either (i) water; (ii) MAL+FRU+PEC+ALG (90 g·h−1 CHO/16% w/v); or (iii) a ratio-matched MAL+FRU drink (90 g·h−1 CHO/16% w/v). Blood was sampled before and after exercise and gastrointestinal (GI) permeability, which was determined by serum measurements of intestinal fatty acid binding protein (I-FABP) and the percent ratio of lactulose (5 g) to rhamnose (2 g) recovered in postexercise urine. Compared with water, I-FABP decreased by 349 ± 67pg·mL−1 with MAL+FRU+PEC+ALG (p = 0.007) and by 427 ± 56 pg·mL−1 with MAL+FRU (p = 0.02). GI permeability was reduced in both the MAL+FRU+PEC+ALG (by 0.019 ± 0.01, p = 0.0003) and MAL+FRU (by 0.014 ± 0.01, p = 0.002) conditions relative to water. In conclusion, both CHO beverages attenuated GI barrier damage to a similar extent relative to water. No metabolic, cardiovascular, thermoregulatory, or performance differences were observed between the CHO beverages.

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Publication

Cross-linking of diluted alkali-soluble pectin from apple (Malus domestica fruit) in different acid-base conditions.

Gawkowska, D., Cieśla, J., Zdunek, A. & Cybulska, J. (2019). Food Hydrocolloids, 92, 285-292.

A diluted alkali-soluble pectin (DASP) fraction, extracted using sodium carbonate, is characterized by a low degree of methylesterification and has the ability to self-organize on mica. The aim of this study was to characterize the cross-linking process of this fraction, extracted from apples, over a wide pH range (3-11) and without the addition of salt. An FT-IR study showed an increase in the intensity of bands connected with νas and νs (COO) and a decrease in the intensity of the band associated with ν (C=O) in the carboxyl group with increasing pH, which indicated the dissociation of the carboxyl groups of galacturonic acid units. An increase in the surface electrical charge of particles in the pH range of 3-7 confirmed this. The value of the average apparent dissociation constant (∼4.60) indicated the acidic character of the DASP fraction. An AFM study showed the morphological changes of the DASP fraction with increasing pH, which allowed for the evaluation of the cross-linking process. This fraction formed a network on mica at pH 4 and 9, while the aggregates were noted mainly at pH 11. For totally ionized carboxyl groups (pH 7), the pectin chains were separated from each other due to the electrostatic repulsion between them.

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Publication

Systemic Concocting of Cross‐Linked Enzyme Aggregates of Candida antarctica Lipase B (Novozyme 435) for the Biomanufacturing of Rhamnolipids.

Rathankumar, A. K., SaiLavanyaa, S., Saikia, K., Gururajan, A., Sivanesan, S., Gosselin, M., Vaidyanathan, V. K. & Cabana, H. (2019). Journal of Surfactants and Detergents, 22(3), 477-490.

In the present study, Candida antarctica lipase B was immobilized on amine‐functionalized silica microspheres as cross‐linked enzyme aggregates (CLEA) and utilized for the biomanufacturing of rhamnolipids (RL). Lipase CLEA synthesized under optimized conditions of 2.0:1.0 by volume of silica microsphere/enzyme concentration, a 1.0:2.5 (v/v) ratio of enzyme/2‐propanol, 7 mM glutaraldehyde concentration, when incubated at pH 9.0 and 40 °C, for a cross‐linking time of 30 min were observed to exhibit superior biocatalytic properties and a maximum enzyme load of 770 U g−1. Lipase CLEA exhibited enhanced pH stability in acidic and alkaline media and increased temperature resistance as compared to free lipase. Both free and CLEA lipases were used to synthesize RL in different solvent systems. After 12 h, from initiation of the esterification, the degree of esterification (molar conversion yield) reached 46% and 71% in the batch mode. 1H and 13C nuclear magnetic resonance (NMR) and high‐performance liquid chromatographic (HPLC) analysis confirm RL production by CLEA lipase. The CLEA showed greater confrontation to enzyme‐mediated bioprocess approach as compared to its soluble counterpart and exhibited excellent RL production and catalytic activity even after its tenth successive reuse.

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Publication

Interactions of anthocyanins with pectin and pectin fragments in model solutions.

Larsen, L. R., Buerschaper, J., Schieber, A. & Weber, F. (2019). Journal of Agricultural and Food Chemistry, 67(33), 9344-9353.

Anthocyanins determine the color and potential health-promoting properties of red fruit juices, but the juices contain remarkably less anthocyanins than the fruits, which is partly caused by the interactions of anthocyanins with the residues of cell wall polysaccharides like pectin. In this study, pectin was modified by ultrasound and enzyme treatments to residues of polysaccharides and oligosaccharides widely differing in their molecular weight. Modifications decreased viscosity and degrees of acetylation and methylation and released smooth and hairy region fragments. Native and modified pectin induced different effects on the concentrations of individual anthocyanins after short-term and long-term incubation caused by both hydrophobic and hydrophilic interactions. Results indicate that both pectin and anthocyanin structure influence these interactions. Linear polymers generated by ultrasound formed insoluble anthocyanin complexes, whereas oligosaccharides produced by enzymes formed soluble complexes with protective properties. The structure of the anthocyanin aglycone apparently influenced interactions more than the sugar moiety.

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Publication
Unusual active site location and catalytic apparatus in a glycoside hydrolase family.

Munoz-Munoz, J., Cartmell, A., Terrapon, N., Henrissat, B. & Gilbert, H. J. (2017). Proceedings of the National Academy of Sciences, 114(19), 4936-4941.

The human gut microbiota use complex carbohydrates as major nutrients. The requirement for an efficient glycan degrading systems exerts a major selection pressure on this microbial community. Thus, we propose that these bacteria represent a substantial resource for discovering novel carbohydrate active enzymes. To test this hypothesis, we focused on enzymes that hydrolyze rhamnosidic bonds, as cleavage of these linkages is chemically challenging and there is a paucity of information on L-rhamnosidases. Here we screened the activity of enzymes derived from the human gut microbiota bacterium Bacteroides thetaiotaomicron, which are up-regulated in response to rhamnose-containing glycans. We identified an α-L-rhamnosidase, BT3686, which is the founding member of a glycoside hydrolase (GH) family, GH145. In contrast to other rhamnosidases, BT3686 cleaved L-Rha-α1,4–D-GlcA linkages through a retaining double-displacement mechanism. The crystal structure of BT3686 showed that the enzyme displayed a type A seven-bladed β-propeller fold. Mutagenesis and crystallographic studies, including the structure of BT3686 in complex with the reaction product GlcA, revealed a location for the active site among β-propeller enzymes cited on the posterior surface of the rhamnosidase. In contrast to the vast majority of GH, the catalytic apparatus of BT3686 does not comprise a pair of carboxylic acid residues but, uniquely, a single histidine functions as the only discernable catalytic amino acid. Intriguingly, the histidine, His48, is not invariant in GH145; however, when engineered into structural homologs lacking the imidazole residue, α-L-rhamnosidase activity was established. The potential contribution of His48 to the catalytic activity of BT3686 is discussed.

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Publication
The effects of acute oral glutamine supplementation on exercise-induced gastrointestinal permeability and heat shock protein expression in peripheral blood mononuclear cells.

Zuhl, M., Dokladny, K., Mermier, C., Schneider, S., Salgado, R. & Moseley, P. (2015). Cell Stress and Chaperones, 20(1), 85-93.

Chronic glutamine supplementation reduces exercise-induced intestinal permeability and inhibits the NF-κB pro-inflammatory pathway in human peripheral blood mononuclear cells. These effects were correlated with activation of HSP70. The purpose of this paper is to test if an acute dose of oral glutamine prior to exercise reduces intestinal permeability along with activation of the heat shock response leading to inhibition of pro-inflammatory markers. Physically active subjects (N = 7) completed baseline and exercise intestinal permeability tests, determined by the percent ratio of urinary lactulose (5 g) to rhamnose (2 g). Exercise included two 60-min treadmill runs at 70 % of VO2max at 30°C after ingestion of glutamine (Gln) or placebo (Pla). Plasma levels of endotoxin and TNF-α, along with peripheral blood mononuclear cell (PBMC) protein expression of HSP70 and IκBα, were measured pre- and post-exercise and 2 and 4 h post-exercise. Permeability increased in the Pla trial compared to that at rest (0.06 ± 0.01 vs. 0.02 ± 0.018) and did not increase in the Gln trial. Plasma endotoxin was lower at the 4-h time point in the Gln vs. 4 h in the Pla (6.715 ± 0.046 pg/ml vs. 7.952 ± 1.11 pg/ml). TNF-α was lower 4 h post-exercise in the Gln vs. Pla (1.64 ± 0.09 pg/ml vs. 1.87 ± 0.12 pg/ml). PBMC expression of IkB TNF-α was higher 4 h post-exercise in the Gln vs. 4 h in the Pla (1.29 ± 0.43 vs. 0.8892 ± 0.040). HSP70 was higher pre-exercise and 2 h post-exercise in the Gln vs. Pla (1.35 ± 0.21 vs. 1.000 ± 0.000 and 1.65 ± 0.21 vs. 1.27 ± 0.40). Acute oral glutamine supplementation prevents an exercise-induced rise in intestinal permeability and suppresses NF-κB activation in peripheral blood mononuclear cells.

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Publication
Effects of oral glutamine supplementation on exercise-induced gastrointestinal permeability and tight junction protein expression.

Zuhl, M. N., Lanphere, K. R., Kravitz, L., Mermier, C. M., Schneider, S., Dokladny, K. & Moseley, P. L. (2014). Journal of Applied Physiology, 116(2), 183-191.

The objectives of this study are threefold: 1) to assess whether 7 days of oral glutamine (GLN) supplementation reduces exercise-induced intestinal permeability; 2) whether supplementation prevents the proinflammatory response; and 3) whether these changes are associated with upregulation of the heat shock response. On separate occasions, eight human subjects participated in baseline testing and in GLN and placebo (PLA) supplementation trials, followed by a 60-min treadmill run. Intestinal permeability was higher in the PLA trial compared with baseline and GLN trials (0.0604 ± 0.047 vs. 0.0218 ± 0.008 and 0.0272 ± 0.007, respectively; P < 0.05). IκBα expression in peripheral blood mononuclear cells was higher 240 min after exercise in the GLN trial compared with the PLA trial (1.411 ± 0.523 vs. 0.9839 ± 0.343, respectively; P < 0.05). In vitro using the intestinal epithelial cell line Caco-2, we measured effects of GLN supplementation (0, 4, and 6 mM) on heat-induced (37°C or 41.8°C) heat shock protein 70 (HSP70), heat shock factor-1 (HSF-1), and occludin expression. HSF-1 and HSP70 levels increased in 6 mM supplementation at 41°C compared with 0 mM at 41°C (1.785 ± 0.495 vs. 0.6681 ± 0.290, and 1.973 ± 0.325 vs. 1.133 ± 0.129, respectively; P < 0.05). Occludin levels increased after 4 mM supplementation at 41°C and 6 mM at 41°C compared with 0 mM at 41°C (1.236 ± 0.219 and 1.849 ± 0.564 vs. 0.7434 ± 0.027, respectively; P < 0.001). GLN supplementation prevented exercise-induced permeability, possibly through HSF-1 activation.

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Safety Information
Symbol : GHS07, GHS08
Signal Word : Danger
Hazard Statements : H315, H319, H360
Precautionary Statements : P201, P202, P264, P280, P302+P352, P305+P351+P338, P337+P313
Safety Data Sheet
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