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Rhizopus oryzae AM16; a new hyperactive L-asparaginase producer: Semi solid-state production and anticancer activity of the partially purified protein

The demand for L-asparaginase is predicted to increase several fold in the future due to its potential clinical applications in the treatment of lymphoid system malignancies and leukemia. Thus identifying suitable sources of production should be considered high priority. Fungi are valuable organisms...

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Detalles Bibliográficos
Autores principales: Othman, Sarah I., Mekawey, Amal A.I., El-Metwally, Mohammad M., Gabr, Sami A., Alwaele, Maha Abdulla, Al Fassam, Haifa, Abo-Eleneen, Rasha, Allam, Ahmed A., Saber, Wesameldin I.A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: D.A. Spandidos 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8814671/
https://www.ncbi.nlm.nih.gov/pubmed/35222999
http://dx.doi.org/10.3892/br.2022.1498
Descripción
Sumario:The demand for L-asparaginase is predicted to increase several fold in the future due to its potential clinical applications in the treatment of lymphoid system malignancies and leukemia. Thus identifying suitable sources of production should be considered high priority. Fungi are valuable organisms as they are able to convert what would be considered ‘useless’ materials into materials that have potential value. The present study provides a proof of concept of production of a new hyperactive L-asparaginase producer (Rhizopus oryzae AM16), which was successfully isolated and sequentially optimized using a semi solid-state fermentation method with a simple and cheap medium produced from wheat bran (WB). The fungus was able to produce an appreciable amount of the enzyme (2,875.9 U) after 8 days of incubation under 85.7% moisture, in the presence of magnesium nitrate (5.0 mg N/mg nitrogen per gram of dry WB) at pH 5.8. Testing the anticancer activity confirmed the ability of the resultant enzyme to inhibit the growth of various types of cancer cells (HepG2, MCF-7, HCT and A549). The IC(50) values of the dialyzed enzyme were lower than that of the crude product. Thus, this newly identified and purified L-asparaginase may be a promising anticancer drug.