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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)
Highly thermostable GH51 α-arabinofuranosidase from Hungateiclostridium clariflavum DSM 19732.
Geng, A., Wu, J., Xie, R., Wang, H., Wu, Y., Li, X., Chang, F. & Sun, J. (2019). Applied microbiology and Biotechnology, 103(9), 3783-3793.
Arabinofuranosidase plays an essential role in the process of hydrolysis of arabinoxylan (AX). Thermostable, versatile, and efficient arabinofuranosidase is thus of great interest for the biorefinery industry. A GH51 arabinofuranosidase, Abf51, from Hungateiclostridium clariflavum DSM 19732 was heterogeneously expressed in Escherichia coli. Abf51 was found to have an optimal pH and temperature of 6.5 and 60°C, respectively, with very high thermostability. At the optimal working temperature (60°C), Abf51 retained over 90% activity after a 2-day incubation and over 60% activity after a 6-day incubation. Abf51 could effectively remove the arabinofuranosyls from three kinds of AX oligosaccharides [23-α-L-arabinofuranosyl-xylotriose (A2XX), 32-α-L-arabinofuranosyl-xylobiose (A3X), and 2333-di-α-L-arabinofuranosyl-xylotriose (A2 + 3XX)], which characterized as either single substitution or double substitution by arabinofuranosyls on terminal xylopyranosyl units. The maximal catalytic efficiency (Kcat/Km) was observed using p-nitrophenyl-α-L-arabinofuranoside (pNPAF) as a substrate (205.0 s−1 mM−1), followed by using A3X (22.8 s−1 mM−1), A2XX (6.9 s−1 mM−1), and A2 + 3XX (0.5 s−1 mM−1) as substrates. Moreover, the presence of Abf51 significantly stimulated the saccharification level of AX (18.5 g L−1) up to six times along with a β-xylanase as well as a β-xylosidase. Interestingly, in our survey of top thermostable arabinofuranosidases, most members were found from GH51, probably due to their owning of (β/α)8-barrel architectures. Our results suggested the great importance of GH51s as candidates for thermostable, versatile, and efficient arabinofuranosidases toward industry application.Hide Abstract
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
Autotransporter‐based surface display of hemicellulases on Pseudomonas putida: new whole‐cell biocatalysts for the production of xylose from biomass.
Schulte, M. F., Tozakidis, I. E. & Jose, J. (2017). ChemCatChem, 9(20), 3955-3964.
The enzymatic depolymerization of xylans into their monomeric sugars by hemicellulases is of great interest from both the ecological and the economical point of view; however, the high costs of these enzymes impede their employment on 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 by flow cytometry. All four enzymes retained their functionality with hydrolytic activities of 48.5 mU mL−1 for XynA towards beechwood xylan, 6 mU mL−1 for XynB towards 4‐nitrophenyl‐β‐D‐xylopyranoside, and 8.6 mU mL−1 and 6.2 mU mL−1 for the two α‐L‐arabinofuranosidases Abf2 and AbfCelf towards 4‐nitrophenyl‐α‐L‐arabinofuranoside, respectively. Measurements were done with cell suspensions of an OD578=1. A mixture of strains displaying the three types of hemicellulases could degrade 2.5 % (w/v) raw arabinoxylan from rye bran to D‐xylose with a yield of 133.5 mg L−1 cell suspension after 24 h.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