Biochemical characterization of an extremely thermostable l-asparaginase from Thermococcus gammatolerans EJ3

- T. gammatoleransl-asparaginase showed maximum activity at 85 °C and pH 8.5.
- The purified enzyme had specific activities of 7622 U mg−1 for l-Asn.
- The enzyme also has catalytic activity toward d-Asn, l-Gln, and d-Gln.
- It displayed promising thermostability and a relatively wide pH spectrum.
- The Km and kcat/Km for l-Asn were 10.0 mM and 572.1 mM−1 s−1, respectively.