α-Fucosidase (Thermotoga maritima)

Reference code: E-FUCTM
SKU: 700004219

10 Units at 25oC

Content: 10 Units at 25oC
Shipping Temperature: Ambient
Storage Temperature: 2-8oC
Formulation: In 3.2 M ammonium sulphate
Physical Form: Suspension
Stability: > 1 year under recommended storage conditions
Enzyme Activity: α-Fucosidase
EC Number: 3.2.1.51
CAZy Family: GH29
CAS Number: 9037-65-4
Synonyms: alpha-L-fucosidase; alpha-L-fucoside fucohydrolase
Source: Thermotoga maritima
Molecular Weight: 54,351
Concentration: Supplied at ~ 5 U/mL
Expression: Recombinant from Thermotoga maritima
Specificity: Hydrolysis of α-L-fucose residues from the non-reducing terminal residues in glycoproteins and oligosaccharides.
Specific Activity: ~ 2.5 U/mg protein (25oC); 
~ 4 U/mg protein (37oC); 
~ 15 U/mg protein (60oC);  
~ 200 U/mg protein (95oC)
Unit Definition: One Unit of α-fucosidase activity is defined as the amount of enzyme required to release one µmole of p-nitrophenol (pNP) per minute from p-nitrophenyl-α-L-fucopyranoside in citrate buffer (50 mM)/phosphate buffer (100 mM), pH 5.0.
Temperature Optima: 95oC
pH Optima: 5
Application examples: For use in glycobiology research.

High purity recombinant α-Fucosidase (Thermotoga maritima) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

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Documents
Certificate of Analysis
Safety Data Sheet
Data Sheet
Publications
Publication

Increasing complexity of the N-glycome during Caenorhabditis development.

Wilson, I. B., Yan, S., Jin, C., Dutkiewicz, Z., Rendić, D., Palmberger, D., Schnabel, R. & Paschinger, K. (2023). Molecular & Cellular Proteomics, 22(3).

Caenorhabditis elegans is a frequently employed genetic model organism and has been the object of a wide range of developmental, genetic, proteomic, and glycomic studies. Here, using an off-line MALDI-TOF-MS approach, we have analyzed the N-glycans of mixed embryos and liquid- or plate-grown L4 larvae. Of the over 200 different annotatable N-glycan structures, variations between the stages as well as the mode of cultivation were observed. While the embryonal N-glycome appears less complicated overall, the liquid- and plate-grown larvae differ especially in terms of methylation of bisecting fucose, α-galactosylation of mannose, and di-β-galactosylation of core α1,6-fucose. Furthermore, we analyzed the O-glycans by LC–electrospray ionization–MS following β-elimination; especially the embryonal O-glycomes included a set of phosphorylcholine-modified structures, previously not shown to exist in nematodes. However, the set of glycan structures cannot be clearly correlated with levels of glycosyltransferase transcripts in developmental RNA-Seq datasets, but there is an indication for coordinated expression of clusters of potential glycosylation-relevant genes. Thus, there are still questions to be answered in terms of how and why a simple nematode synthesizes such a diverse glycome.

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Publication

Root-knot nematode chemotaxis is positively regulated by L-galactose sidechains of mucilage carbohydrate rhamnogalacturonan-I.

Tsai, A. Y. L., Iwamoto, Y., Tsumuraya, Y., Oota, M., Konishi, T., Ito, S., Kotake, T., Ishikawa, H. & Sawa, S. (2021). Science Advances, 7(27), eabh4182.

Root-knot nematodes (RKNs) are plant parasites and major agricultural pests. RKNs are thought to locate hosts through chemotaxis by sensing host-secreted chemoattractants; however, the structures and properties of these attractants are not well understood. Here, we describe a previously unknown RKN attractant from flaxseed mucilage that enhances infection of Arabidopsis and tomato, which resembles the pectic polysaccharide rhamnogalacturonan-I (RG-I). Fucose and galactose sidechains of the purified attractant were found to be required for attractant activity. Furthermore, the disaccharide α-L-galactosyl-1,3-L-rhamnose, which forms the linkage between the RG-I backbone and galactose sidechains of the purified attractant, was sufficient to attract RKN. These results show that the α-L-galactosyl-1,3-L-rhamnose linkage in the purified attractant from flaxseed mucilage is essential for RKN attraction. The present work also suggests that nematodes can detect environmental chemicals with high specificity, such as the presence of chiral centers and hydroxyl groups.

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Publication

Development of a 1, 2-difluorofucoside activity-based probe for profiling GH29 fucosidases.

Luijkx, Y. M., Jongkees, S., Strijbis, K. & Wennekes, T. (2021). Organic & Biomolecular Chemistry, 19(13), 2968-2977.

GH29 α-L-fucosidases catalyze hydrolysis of terminal α-L-fucosyl linkages with varying specificity and are expressed by prominent members of the human gut microbiota. Both homeostasis and dysbiosis at the human intestinal microbiota interface have been correlated with altered fucosidase activity. Herein we describe the development of a 2-deoxy-2-fluoro fucosyl fluoride derivative with an azide mini-tag as an activity-based probe (ABP) for selective in vitro labelling of GH29 α-L-fucosidases. Only catalytically active fucosidases are inactivated by this ABP, allowing their functionalization with a biotin reporter group via the CuAAC reaction and subsequent in-gel detection at nanogram levels. The ABP we present here is shown to be active against a GH29 α-L-fucosidase from Bacteroides fragilis and capable of labeling two other GH29 α-L-fucosidases with different linkage specificity, illustrating its broader utility. This novel ABP is a valuable addition to the toolbox of fucosidase probes by allowing identification and functional studies of the wide variety of GH29 fucosidases, including those in the gut microbiota.

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Publication
Improvement of the transfucosylation activity of α-L-fucosidase from Thermotoga maritima for the synthesis of fucosylated oligosaccharides in the presence of calcium and sodium.

Guzmán-Rodríguez, F., Alatorre-Santamaría, S., Gómez-Ruiz, L., Rodríguez-Serrano, G., García-Garibay, M. & Cruz-Guerrero, A. (2018). Extremophiles, 1-6.

The influence of CaCl2 and NaCl in the hydrolytic activity and the influence of CaCl2 in the synthesis of fucosylated oligosaccharides using α-L-fucosidase from Thermotoga maritima were evaluated. The hydrolytic activity of α-L-fucosidase from Thermotoga maritima displayed a maximum increase of 67% in the presence of 0.8 M NaCl with water activity (aw) of 0.9672 and of 138% in the presence of 1.1 M CaCl2 (aw 0.9581). In addition, the hydrolytic activity was higher when using CaCl2 compared to NaCl at aw of 0.8956, 0.9581 and 0.9672. On the other hand, the effect of CaCl2 in the synthesis of fucosylated oligosaccharides using 4-nitrophenyl-fucose as donor substrate and lactose as acceptor was studied. In these reactions, the presence of 1.1 M CaCl2 favored the rate of transfucosylation, and improved the yield of synthesis duplicating and triplicating it with lactose concentrations of 58 and 146 mM, respectively. CaCl2 did not significatively affect hydrolysis rate in these reactions. The combination of the activating effect of CaCl2, the decrement in aw and lactose concentration had a synergistic effect favoring the synthesis of fucosylated oligosaccharides.

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Safety Information
Symbol : Not Applicable
Signal Word : Not Applicable
Hazard Statements : Not Applicable
Precautionary Statements : Not Applicable
Safety Data Sheet
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