Content: | 400 Units at 25oC |
Shipping Temperature: | Ambient |
Storage Temperature: | 2-8oC |
Formulation: | In 2.5 M lithium sulphate |
Physical Form: | Suspension |
Stability: | > 4 years at 4oC |
Enzyme Activity: | Other Activities |
EC Number: | 3.5.1.1 |
CAS Number: | 9015-68-3 |
Synonyms: | asparaginase; L-asparagine amidohydrolase |
Source: | Escherichia coli |
Molecular Weight: | 37,900 |
Concentration: | Supplied at ~ 350 U/mL |
Expression: | Recombinant from Escherichia coli |
Specificity: |
Catalyses the reaction: L-Asparagine + H2O = L-aspartate + NH3 |
Specific Activity: |
~ 15 U/mg (25oC, pH 8.0 on L-asparagine); ~ 30 U/mg (37oC, pH 8.0 on L-asparagine) |
Unit Definition: | One Unit of asparaginase activity is defined as the amount of enzyme required to produce one µmole of L-aspartate from L-asparagine (7.3 mM) per minute in the presence of NADPH in Tris.HCL buffer (45 mM), pH 8.0. |
Temperature Optima: | 37oC |
pH Optima: | 8 |
Application examples: | Applications established for the measurement of asparagine in the food, fermentation, wine, beverage, medical and pharmacological industries. |
This product has been discontinued (read more).
High purity recombinant Asparaginase (Escherichia coli) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
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Liu, X., Tian, M., Camara, M. A., Guo, L. & Yang, L. (2015). Electrophoresis, 36(19), 2380-2385.
We present sequential CE analysis of amino acids and L-asparaginase-catalyzed enzyme reaction, by combing the on-line derivatization, optically gated (OG) injection and commercial-available UV-Vis detection. Various experimental conditions for sequential OG-UV/vis CE analysis were investigated and optimized by analyzing a standard mixture of amino acids. High reproducibility of the sequential CE analysis was demonstrated with RSD values (n = 20) of 2.23, 2.57, and 0.70% for peak heights, peak areas, and migration times, respectively, and the LOD of 5.0 µM (for asparagine) and 2.0 µM (for aspartic acid) were obtained. With the application of the OG-UV/vis CE analysis, sequential online CE enzyme assay of L-asparaginase-catalyzed enzyme reaction was carried out by automatically and continuously monitoring the substrate consumption and the product formation every 12 s from the beginning to the end of the reaction. The Michaelis constants for the reaction were obtained and were found to be in good agreement with the results of traditional off-line enzyme assays. The study demonstrated the feasibility and reliability of integrating the OG injection with UV/vis detection for sequential online CE analysis, which could be of potential value for online monitoring various chemical reaction and bioprocesses.
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