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- W2049393571 abstract "Microbial l-asparaginases which catalyze the conversion of l-asparagine to l-asparate and ammonia, have been proved to be useful in medical and food industries. In the present work, a thermostable l-asparaginase was characterized from a hyperthermophilic archaeon strain, Thermococcus gammatolerans EJ3. Cloning and recombinant expression of Tco. gammatolerans l-asparaginase was performed in Escherichia coli. The recombinant enzyme was purified to homogeneity by nickel-affinity chromatography, and was characterized as a homodimer composed of two identical subunits of approximately 36.5 kDa. The optimum pH and temperature were 8.5 and 85 °C, respectively. The purified enzyme had specific activities of 7622 and 2926 U mg−1 for l-asparagine and l-glutamine, respectively, and exhibited promising thermostability at all tested temperatures from 70 to 95 °C. In addition, it displayed very high catalytic efficiency toward substrate l-asparagine. The Michaelis–Menten constant (Km), turnover number (kcat), and catalytic efficiency (kcat/Km) values for substrate l-asparagine were estimated to be 10.0 mM, 5721 s−1, and 572.1 mM−1 s−1, respectively." @default.
- W2049393571 created "2016-06-24" @default.
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- W2049393571 date "2014-11-01" @default.
- W2049393571 modified "2023-10-17" @default.
- W2049393571 title "Biochemical characterization of an extremely thermostable l-asparaginase from Thermococcus gammatolerans EJ3" @default.
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- W2049393571 doi "https://doi.org/10.1016/j.molcatb.2014.08.021" @default.
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