@article{open3055,
          volume = {58},
          number = {4},
           month = {July},
          author = {S. Chand and K. N. Mihooliya and D. K. Sahoo and J. P. Prasad and G. Sharma},
            note = {The copyright of this article belongs to Springer },
           title = {L-asparaginase from Bacillus flexus strain SS: Isolation, Screening, Production Process Optimization, Purification, and Anticancer Activity},
       publisher = {Springer },
            year = {2022},
         journal = {APPLIED BIOCHEMISTRY AND MICROBIOLOGY},
           pages = {416--427},
             url = {http://crdd.osdd.net/open/3055/},
        abstract = {L-asparaginase has been widely accepted as a standard anticancer drug for acute lymphoblastic leukaemia (ALL). Presently in L-asparaginase biotherapeutic applications, the main focus is developing new L-asparaginase with minimal or without any glutaminase activity to reduce the associated adverse drug reactions. In this study, Bacillus flexus strain SS (NCBI GenBank Accession Number MN420983) was identified as a promising producer of L-asparaginase. L-asparaginase production was optimized by response surface methodology statistical bioprocess modelling, and enzyme yield of 25.08 IU/mL was reached at the bioreactor scale. The purification of L-asparaginase included ammonium sulfate precipitation, ion-exchange chromatography and size exclusion chromatography yielding 5.27-fold purification. The SDS-PAGE and CE-SDS revealed the monomeric L-asparaginase with molecular weight of 33 kDa. The purified enzyme was highly specific to substrate L-Asn and free from glutaminase activity. The anticancer activity of purified L-asparaginase was found specific against tumor cell lines SKBR3 (IC50 = 0.8 ?g/mL), WIL2-S (IC50 = 16.2 ?g/mL), and TF-1 (IC50 = 47 ?g/mL), but not against negative control HUVEC cells. Therefore, L-asparaginase from B. flexus SS with no glutaminase activity could be a potential new candidate for anticancer drug for ALL with reduced adverse effects.}
}