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- W4366991963 abstract "Abstract L-asparaginase is an antileukemic enzyme that hydrolyzes L-asparagine into L-aspartic acid and ammonia, causing leukemia cell starvation and apoptosis in susceptible leukemic cell populations. Currently, L-asparaginase obtained from bacterial sources is constrained by several issues, including lesser productivity, stability, selectivity, and higher toxicity. The goal of this study is to provide fungal L-asparaginase with in-vitro effectiveness towards different human carcinomas. L-asparaginase from endophytic Fusarium solani (Gene Bank accession number MW209717) isolated from the roots of the medicinal plant Hedera helix L. was characterized and optimized experimentally for maximum L-asparaginase production in addition to evaluating its subsequent cytotoxicity towards acute monocytic leukemia and human skin fibroblast cell lines. The enzyme production was maximized using potato dextrose media at the 5 th and 6 th days of fermentation with incubation temperature 30 ℃ with 3% asparagine. Enzyme characterization studies revealed that the enzyme maintained its thermal stability with temperatures up to 60 ℃. Results revealed promising cytotoxic activity against acute monocytic leukemia with IC 50 = 3.66 µg/ml with low cytotoxicity against tested normal human skin fibroblast cell line which suggested that it might have selective toxicity, and consequently it could be used as a less toxic alternative to the current formulations." @default.
- W4366991963 created "2023-04-27" @default.
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- W4366991963 date "2023-04-25" @default.
- W4366991963 modified "2023-09-26" @default.
- W4366991963 title "Optimization and characterization of antileukemic L-asparaginase produced by Fusarium solani endophyte" @default.
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- W4366991963 doi "https://doi.org/10.21203/rs.3.rs-2791390/v1" @default.
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