PRODUCTION AND CHARACTERISATION OF L-ASPARAGINASE FROM Priestia megaterium GAFA

dc.contributor.authorFasiku Samuel Adedayo
dc.contributor.authorOladunni Atilade Amos
dc.contributor.authorOkpala Gift Chimamaka
dc.contributor.authorFasiku Taiwo Bukola
dc.contributor.authorAfolabi Femi Johnson
dc.date.accessioned2026-02-23T11:32:55Z
dc.date.available2026-02-23T11:32:55Z
dc.date.issued2026-02-20
dc.description.abstractL-asparaginase is an enzyme used to treat acute lymphoblastic leukaemia due to its ability to break downexternal L-asparagine necessary for the growth of cancer cells. This work investigated the optimisation of Lasparaginase production and the effect of various factors on the activities of the produced enzyme. An Lasparaginase-producing bacterium collected from the Department of Microbiology and Biotechnology Laboratory was identified using 16S rRNA. The production of L-asparaginase was optimised using Response Surface Methodology (RSM), and the experimental design was validated. The effect of environmental factors on L-asparaginase was determined. The L-asparagine-producing bacterium was identified as Priestia megaterium GAFA with an accession number PP390497. Optimal production (10594.1 U/mL) was validated using glucose as a carbon source, L-asparaginase only as a nitrogen source, fermented at pH 7.76 for 73 hours with an inoculum load of 7.7%. The Ca²⁺ ion significantly increased L-asparaginase activity by 76% compared with the control at p<0.05. The enzyme was active over a wide pH range (4–8), with maximum activity at pH 6.0. The highest activity was observed at 60 °C after 1 hour of incubation. The production of L-asparaginase by Priestia megaterium GAFA was optimised, and environmental factors influenced its activity.
dc.identifier.urihttps://repository.acu.edu.ng/handle/123456789/1848
dc.language.isoen
dc.subjectEnvironmental Factors
dc.subjectFermentation
dc.subjectMicrobial Enzymes
dc.subjectOptimisation
dc.subjectResponse Surface Methodology
dc.titlePRODUCTION AND CHARACTERISATION OF L-ASPARAGINASE FROM Priestia megaterium GAFA
dc.typeArticle

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