{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T02:18:53Z","timestamp":1789957133276,"version":"4.0.1"},"reference-count":296,"publisher":"MDPI AG","issue":"20","license":[{"start":{"date-parts":[[2023,10,16]],"date-time":"2023-10-16T00:00:00Z","timestamp":1697414400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Ministry of Education and Science of the Russian Federation","award":["075-15-2021-933"],"award-info":[{"award-number":["075-15-2021-933"]}]},{"name":"Ministry of Education and Science of the Russian Federation","award":["RF00121X0004"],"award-info":[{"award-number":["RF00121X0004"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Genetic engineering for heterologous expression has advanced in recent years. Model systems such as Escherichia coli, Bacillus subtilis and Pichia pastoris are often used as host microorganisms for the enzymatic production of L-asparaginase, an enzyme widely used in the clinic for the treatment of leukemia and in bakeries for the reduction of acrylamide. Newly developed recombinant L-asparaginase (L-ASNase) may have a low affinity for asparagine, reduced catalytic activity, low stability, and increased glutaminase activity or immunogenicity. Some successful commercial preparations of L-ASNase are now available. Therefore, obtaining novel L-ASNases with improved properties suitable for food or clinical applications remains a challenge. The combination of rational design and\/or directed evolution and heterologous expression has been used to create enzymes with desired characteristics. Computer design, combined with other methods, could make it possible to generate mutant libraries of novel L-ASNases without costly and time-consuming efforts. In this review, we summarize the strategies and approaches for obtaining and developing L-ASNase with improved properties.<\/jats:p>","DOI":"10.3390\/ijms242015220","type":"journal-article","created":{"date-parts":[[2023,10,16]],"date-time":"2023-10-16T05:43:49Z","timestamp":1697435029000},"page":"15220","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":38,"title":["Engineering and Expression Strategies for Optimization of L-Asparaginase Development and Production"],"prefix":"10.3390","volume":"24","author":[{"given":"Anastasiya N.","family":"Shishparenok","sequence":"first","affiliation":[{"name":"Laboratory of Medical Biotechnology, Institute of Biomedical Chemistry, Pogodinskaya St. 10\/8, 119121 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yulia A.","family":"Gladilina","sequence":"additional","affiliation":[{"name":"Laboratory of Medical Biotechnology, Institute of Biomedical Chemistry, Pogodinskaya St. 10\/8, 119121 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4753-7588","authenticated-orcid":false,"given":"Dmitry D.","family":"Zhdanov","sequence":"additional","affiliation":[{"name":"Laboratory of Medical Biotechnology, Institute of Biomedical Chemistry, Pogodinskaya St. 10\/8, 119121 Moscow, Russia"},{"name":"Department of Biochemistry, Peoples\u2019 Friendship University of Russia named after Patrice Lumumba (RUDN University), Miklukho\u2014Maklaya St. 6, 117198 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,10,16]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Pokrovskaya, M.V., Pokrovsky, V.S., Aleksandrova, S.S., Sokolov, N.N., and Zhdanov, D.D. 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