|Content:||10 Units on ethyl ferulate|
|Formulation:||In 3.2 M ammonium sulphate|
|Stability:||Minimum 1 year at 4oC. Check vial for details.|
|Synonyms:||feruloyl esterase; 4-hydroxy-3-methoxycinnamoyl-sugar hydrolase|
|Concentration:||Supplied at ~ 7 U/mL|
|Expression:||Recombinant from Clostridium thermocellum|
|Specificity:||Catalyses the hydrolysis of the 4-hydroxy-3-methoxycinnamoyl (feruloyl) group from an esterified sugar, which is usually arabinose in "natural" substrates.|
~ 0.6 U/mg (50oC, pH 6.0 on ethyl ferulate);
~ 28 U/mg (60oC, pH 6.0 on FAXX)
|Unit Definition:||One Unit of feruloyl esterase activity is defined as the amount of enzyme required to release one µmole of ferulic acid per minute from ethyl-ferulate (0.39 mM) in MOPS buffer (100 mM), pH 6.0.|
|Application examples:||Applications established in biofuels, paper and pulp, food, nutrition, medical and pharmacological industries.|
High purity recombinant Feruloyl esterase (Clostridium thermocellum) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
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Metagenomic discovery of feruloyl esterases from rumen microflora.
Wong, D. W., Chan, V. J. & Liao, H. (2019). Applied Microbiology and Biotechnology, 103(20), 8449-8457.
Feruloyl esterases (FAEs) are a key group of enzymes that hydrolyze ferulic acids ester-linked to plant polysaccharides. The cow’s rumen is a highly evolved ecosystem of complex microbial microflora capable of converting fibrous substances to energy. From direct cloning of the rumen microbial metagenome, we identified seven active phagemids conferring feruloyl esterase activity. The genomic inserts ranged from 1633 to 4143 bp, and the ORFs from 681 to 1359 bp. BLAST search reveals sequence homology to feruloyl esterases and esterases/lipases identified in anaerobes. The seven genes were expressed in Escherichia coli, and the proteins were purified to homogeneity. The FAEs were found to cover types B, C, and D in the feruloyl esterase classification system using model hydroxycinnamic acid esters. The release of ferulic acid (FA) catalyzed by these enzymes was established using natural substrates corn fiber (CF) and wheat insoluble arabinoxylan (WIA). Three of the enzymes were demonstrated to cleave diferulates and hence the capability to break down Araf-FA-FA-Araf cross-links. The wide variation in the sequence, activity, and substrate specificity observed in the FAEs discovered in this study is a confirming evidence that combined actions of a full range of FAE enzymes contribute to the high-efficiency fiber digestion in the rumen microbial ecosystem.Hide Abstract
Snelders, J., Dornez, E., Broekaert, W. F., Delcour, J. A. & Courtin, C. M. (2013). Bioactive Carbohydrates and Dietary Fibre, 2(1), 84-91.
Arabinoxylan-oligosaccharide samples (AXOS) present themselves as mixtures of different molecular entities with xylan backbones of different length and with different levels of arabinose substitution. Their prebiotic properties depend on their degree of polymerisation (DP) and degree of arabinose substitution (DAS). Therefore, structural characterisation of AXOS samples is important. Gas chromatography (GC) is most frequently used for quantification of AXOS levels and for determination of the average DP (avDP) and average DAS (avDAS), yet it does not provide information on the molecular mass distribution of the xylan backbones of the different AXOS entities present in the mixture. This manuscript evaluates a method based on high performance anion exchange chromatography (HPAEC) involving quantification of xylo-oligosaccharides (XOS) after either acidic or enzymic removal of arabinose substituents for its ability to determine such distribution. Results show that despite the fact that a small fraction of the arabinoses could not be removed, representative DP distributions of xylan backbones in complex AXOS samples were obtained. The similarity of the avDP determined with GC or determined with the new HPAEC method using enzymic removal of arabinose substituents confirmed this. It can be concluded that the HPAEC method involving enzymic removal of arabinoses provides useful insight in the DP distribution of the xylan backbones in complex AXOS samples.Hide Abstract