100 assays per kit
Prices exclude VAT
Available for shipping
|Content:||100 assays per kit|
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|
The Arabinan test kit is suitable for the measurement and analysis of Arabinan in fruit juice concentrates.
- 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
(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)
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
Schwartz, J. M., Solé, V., Guéguen, J., Ropers, M. H., Riaublanc, A. & Anton, M. (2015). LWT-Food Science and Technology, 63(1), 562-568.
Environmental, demographic and economic motives draw a worldwide tendency to introduce plant proteins into processed foods. However the total replacement of animal proteins by plant proteins is not easy to perform due to the specific physicochemical properties (aggregation, solubility, interactions …) and taste of these proteins. In a first step, combined plant/animal assemblies could be an attractive approach. Consequently, to drive this trend towards practical applications, deeper investigations must be performed to control the properties of such mixed assemblies. In the current study, the interactions of β-casein with napin, a rapeseed protein poorly valorized in human nutrition, was investigated in various physico-chemical conditions (pH, sodium chloride concentration, mass ratio). The properties of the mix were followed by turbidimetry, and microscopy. The statistical analysis of the whole set of data indicated that the effects of the three factors were significant (p < 0.05) without significant cross effects. Furthermore, the aggregation is enhanced by temperature with a reversible effect. The aggregation is also suppressed by adding salt or divalent cation chelating agents (ethylene diamine tetracetic acid, EDTA). The functional combination of β-casein with napin can thus be controlled by modulating the salinity of the media and/or by introducing a complexing agent.Hide Abstract