Identification of a thermostable L-asparaginase from Pyrococcus yayanosii CH1 and its application in the reduction of acrylamide

L-asparaginase (ASNase, E.C. 3.5.1.1) catalyzes the deamination of L-asparagine to L-aspartic acid and ammonia and is widely used in medicine to treat acute lymphocytic leukemia. It also has significant applications in the food industry by inhibiting acrylamide formation. In this study, we characterized a thermostable ASNase from the hyper thermophilic strain, Pyrococcus yayanosii CH1. The recombinant enzyme (PyASNase) exhibited maximal activity at pH 8.0 and 85 degrees C. Moreover, PyASNase demonstrated promising thermostability across temperatures ranging from 70 to 95 degrees C. The kinetic parameters of PyASNase for L-asparagine were a K-m of 6.3 mM, a k(cat) of 1989s(-1), and a k(cat)/K-m of 315.7 mM(-1) s(-1). Treating potato samples with 10 U/mL of PyASNase at 85 degrees C for merely 10 min reduced the acrylamide content in the final product by 82.5%, demonstrating a high efficiency and significant advantage of PyASNase in acrylamide inhibition.