α-Fucosidase (Thermotoga maritima)
10 Units at 25oC
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| Content: | 10 Units at 25oC |
| Shipping Temperature: | Ambient |
| Storage Temperature: | 2-8oC |
| Formulation: | In 3.2 M ammonium sulphate |
| Physical Form: | Suspension |
| Stability: | > 4 years at 4oC |
| 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.
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.
Hide Abstract| Symbol : | Not Applicable |
| Signal Word : | Not Applicable |
| Hazard Statements : | Not Applicable |
| Precautionary Statements : | Not Applicable |
