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ʟ-asparaginases and their potential in biotechnology and medicine

Lucie Pejšková, Karolína Loužecká, Tomáš Podzimek, Eva Benešová

. 2023 ; 117 (8) : 508-515.

Jazyk angličtina Země Česko

Typ dokumentu přehledy

Perzistentní odkaz   https://www.medvik.cz/link/bmc24003919

ʟ-Asparaginase (EC 3.5.1.1) is a key enzyme that hydrolyzes ʟ-asparagine to ʟ-aspartic acid and ammonia. This feature of ʟ-asparaginase is used in anti‐cancer therapy to inhibit protein synthesis in cancer cells. Therefore, ʟ-asparaginase is used as a basis for chemotherapy to treat patients with acute lymphoblastic leukemia in pediatrics. Commercial ʟ-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 ʟ-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, ʟ-asparaginase has become indispensable for the food industry in recent years, when it had been recognized as one of the possible tools for removing ʟ-asparagine from foods that are at risk of acrylamide formation during thermal processing. This review provides an overview of the current use of ʟ-asparaginase and its pitfalls.

Citace poskytuje Crossref.org

Bibliografie atd.

Literatura

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