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|Storage Temperature:||Below -10oC|
|Stability:||> 10 years under recommended storage conditions|
|Substrate For (Enzyme):||α-Arabinofuranosidase|
|Assay Format:||Spectrophotometer, Microplate, Auto-analyser|
High purity 4-Nitrophenyl-α-L-arabinofuranoside for use in research, biochemical enzyme assays and in vitro diagnostic analysis. This is a colourimetric substrate for the measurement of α-L-arabinofuranosidase activity.
(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)
Liang, D., Gong, L., Yao, B., Xue, X., Qin, X., Ma, R., Luo, H., Xie, X., Su, X. & Su, X. (2015). Biochemical and biophysical research communications, 467(2), 334-340.
Many glycoside hydrolases involved in deconstruction of cellulose and xylan from the excellent plant cell wall polysaccharides-degrader Caldicellulosiruptor bescii have been cloned and analyzed. However, far less is known about the enzymatic breakdown of mannan, an important component of hemicellulose. We herein cloned, expressed and purified the first β-mannosidase CbMan2A from C. bescii. CbMan2A is thermophilic, with an optimal temperature of 80°C. CbMan2A hydrolyzes mannooligosaccharides with degrees of polymerization from 2 to 6 mainly into mannose and shows strong synergy with CbMan5A, an endo-mannanase from the same bacterium, in releasing mannose from β-1,4-mannan. Thus CbMan2A forms the missing link in enzymatic conversion of mannan into the ready-to-use mannose by C. bescii. Based on these observations, a model illustrating how CbMan2A may assist C. bescii in mannan utilization is presented. In addition, CbMan2A appeared to bind to insoluble galactomannan in a pH-dependent fashion. Although the relation of this feature to mannan utilization remains elusive, CbMan2A represents an excellent model for investigation of the binding of GH2 β-mannosidases to galactomannan.Hide Abstract
Schulte, M. F., Tozakidis, I. E. & Jose, J. ChemCatChem, 9(20), 3955-3964.
The enzymatic depolymerization of xylans into their monomeric sugars by hemicellulases is of great interest both from the ecological and the economical point of view, however the high costs of these enzymes currently impede their employment in industrial scales. The utilization of whole cells displaying the enzymes on their surface could reduce costs by allowing a direct employment of the cells after cultivation and their reuse in multiple reaction cycles. Here, we present the surface display of an endo-1,4-β-xylanase (XynA), a 1,4-β-xylosidase (XynB) and two α-L-arabinofuranosidases (Abf2 and AbfCelf) in the Gram-negative soil bacterium Pseudomonas putida KT2440 by fusing the enzymes to the EhaA autotransporter unit from Escherichia coli. The surface display of the enzymes was verified via flow cytometry. All four enzymes retained their functionality with hydrolytic activities of 48.5 mU/mL for XynA towards beechwood xylan, 6 mU/mL for XynB towards 4-nitrophenyl-β-D-xylopyranoside, 8.6 mU/mL and 6.2 mU/mL for the two α-L-arabinofuranosidases Abf2 and AbfCelf towards 4-nitrophenyl-α-L-arabinofuranoside. Measurements were done with cell suspensions of an OD578 = 1. A mixture of strains displaying the three types of hemicellulases was able to degrade 2.5 % (w/v) raw arabinoxylan from rye bran to D-xylose with a yield of 133.5 mg per L cell suspension after 24 hours.Hide Abstract
Shahid, S., Tajwar, R. & Akhtar, M. W. (2017). Extremophiles, 1-11.
A novel, family GH10 enzyme, Xyn10B from Acidothermus cellulolyticus 11B was cloned and expressed in Escherichia coli. This enzyme was purified to homogeneity by binding to regenerated amorphous cellulose. It had higher binding on Avicel as compared to insoluble xylan due to the presence of cellulose-binding domains, CBM3 and CBM2. This enzyme was optimally active at 70°C and pH 6.0. It was stable up to 70°C while the CD spectroscopy analysis showed thermal unfolding at 80°C. Xyn10B was found to be a trifunctional enzyme having endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities. Its activities against beechwood xylan, p-Nitrophenyl arabinofuranoside and p-Nitrophenyl acetate were found to be 126,480, 10,350 and 17,250 U µmol-1, respectively. Xyn10B was highly active producing xylobiose and xylose as the major end products, as well as debranching the substrates by removing arabinose and acetyl side chains. Due to its specific characteristics, this enzyme seems to be of importance for industrial applications such as pretreatment of poultry cereals, bio-bleaching of wood pulp and degradation of plant biomass.Hide Abstract