L-Asparaginases and Their Potential in Biotechnology and Medicine

L-Asparaginase (EC 3.5.1.1) is a key enzyme that hydrolyzes L-asparagine to L-aspartic acid and ammonia. This feature of L-asparaginase is used in anti-cancer therapy to inhibit protein synthesis in cancer cells. Therefore, L-asparaginase is used as a basis for chemotherapy to treat patients with acute lymphoblastic leukemia in pediatrics. Commercial L-asparaginases for healthcare applications are mainly obtained from Escherichia coli and Erwinia chrysanthemi (renamed to Dickeya dadantii). However, the high prevalence of adverse effects complicates the long-term clinical use of L-asparaginase, and therefore current research focuses on the search for new enzymes or on modifying the properties of enzymes already known. At the same time, L-asparaginase has become indispensable for the food industry in recent years, when it had been recognized as one of the possible tools for removing L-asparagine from foods that are at risk of acrylamide formation during thermal processing. This review provides an overview of the current use of L-asparaginase and its pitfalls.