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|Storage Temperature:||Below -10oC|
|Stability:||> 10 years under recommended storage conditions|
|Substrate For (Enzyme):||β-Xylosidase|
|Assay Format:||Spectrophotometer, Microplate, Auto-analyser|
This product has been discontinued (read more).
High purity 4-Nitrophenyl-β-D-xylopyranoside for use in research, biochemical enzyme assays and in vitro diagnostic analysis. This is a colourimetric substrate for the measurement of β-xylosidase activity.
More products available on our colourimetric substrates product list.
Innovative microscale workflow from fungi cultures to Cell Wall‐Degrading Enzyme screening.
Raulo, R., Heuson, E., Siah, A., Phalip, V. & Froidevaux, R. (2019). Microbial Biotechnology, 12(6), 1286-1292.
This study aimed at developing a complete miniaturized high‐throughput screening workflow for the evaluation of the Cell Wall‐Degrading Enzyme (CWDE) activities produced by any fungal strain directly cultivated on raw feedstock in a submerged manner. In this study, wheat straw was selected as model substrate as it represents an important carbon source but yet poorly valorised to yield high added value products. Fungi were grown in a microbioreactor in a high‐throughput (HT) way to replace the fastidious shaking flask cultivations. Both approaches were compared in order to validate our new methodology. The range of CWDE activities produced from the cultures was assayed using AZO‐died and pNP‐linked substrates in an SBS plate format using a Biomek FXp pipetting platform. As highlighted in this study, it was shown that the CWDE activities gathered from the microbioreactor cultivations were similar or higher to those obtained from shake flasks cultures, with a lower standard deviation on the measured values, making this new method much faster than the traditional one and suitable for HT CWDE production thanks to its pipetting platform compatibility. Also, the results showed that the enzymatic activities measured were the same when doing the assay manually or using the automated method.Hide Abstract
AL-Darkazali, H., Meevootisom, V., Isarangkul, D. & Wiyakrutta, S. (2017). International Journal of Microbiology, 2017, ID 4018398.
A xylanase gene xynAMG1 with a 1,116-bp open reading frame, encoding an endo-β-1,4-xylanase, was cloned from a chicken cecum metagenome. The translated protein XynAMG1 consisted of 372 amino acids including a putative signal peptide of 23 amino acids. The calculated molecular mass of the mature XynAMG1 was 40,013 Da, with a theoretical pI value of 5.76. The amino acid sequence of XynAMG1 showed 59% identity to endo-β-1,4-xylanase from Prevotella bryantii and Prevotella ruminicola and 58% identity to that from Prevotella copri. XynAMG1 has two conserved motifs, DVVNE and TEXD, containing two active site glutamates and an invariant asparagine, characteristic of GH10 family xylanase. The xynAMG1 gene without signal peptide sequence was cloned and fused with thioredoxin protein (Trx.Tag) in pET-32a plasmid and overexpressed in Escherichia coli TunerTM (DE3)pLysS. The purified mature XynAMG1 was highly salt-tolerant and stable and displayed higher than 96% of its catalytic activity in the reaction containing 1 to 4 M NaCl. It was only slightly affected by common organic solvents added in aqueous solution to up to 5 M. This chicken cecum metagenome-derived xylanase has potential applications in animal feed additives and industrial enzymatic processes requiring exposure to high concentrations of salt and organic solvents.Hide Abstract