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. 2022 Apr;29(18):27283-27293.
doi: 10.1007/s11356-021-17925-1. Epub 2022 Jan 3.

Plant asparaginase versus microbial asparaginase as anticancer agent

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Plant asparaginase versus microbial asparaginase as anticancer agent

Nawal E Al-Hazmi et al. Environ Sci Pollut Res Int. 2022 Apr.

Abstract

The considerable effect of enzymes on human health draws great attention to enzyme-based drugs (therapeutic enzymes), in recent times. L-asparaginase (ASNase) is a well-known therapeutic enzyme. It has varied applications and is a single molecule for the treatment of multiple diseases. This study tries to extract asparaginase from soybean debris (agricultural wastes) as a cheap plant source and compare this with microbial asparaginase as an agent in cancer chemotherapy. The asparaginase was extracted and purified from soybean debris (plant asparaginase) and Pseudomonas aeruginosa (microbial asparaginase), then the physiochemical characters were determined for the two enzymes, and the anticancer activity of plant and microbial asparaginase was determined against gastric cancer (CLS-145), pancreatic cancer (AsPC-1), colon cancer (HCT116), esophagus cancer (KYSE-410), liver cancer (HepG2), breast cancer (MCF-7), and cervical cancer (HELLA). The results showed that plant asparaginase was superior to microbial asparaginase in its physiochemical characters. Plant asparaginase showed higher stability and activity under the conditions of changing either the temperature or the pH; also plant asparaginase has a higher affinity to the asparagine than the microbial asparaginase; besides, this plant asparaginase did not show activity with glutamine as a substrate. The plant asparaginase showed higher anticancer activity than that of microbial asparaginase against all studied cancer cell lines. The present study introduces as the first time a comparative study between the plant and microbial asparaginase which proves that soybean debris asparaginase can be more efficient and safe than that of the microbial asparaginase as an anticancer agent.

Keywords: Anticancer activity; Pseudomonas aeruginosa; Soybean debris; Thermal stability; pH stability.

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References

    1. Adeola HA, Bano A, Vats R, Vashishtha A, Verma D, Kaushik D, Mittal V, Rahman MDH, Najda A, Albadrani GM, Sayed AA, Farouk SM, Hassanein EHM, Akhtar MF, Saleem A, Abdel-Daim MM, Bhardwaj R (2021) Bioactive compounds and their libraries: an insight into prospective phytotherapeutics approach for oral mucocutaneous cancers. Biom Pharmacother 141:111809. https://doi.org/10.1016/j.biopha.2021.111809 - DOI
    1. Al Yousef SA (2021) Fusarium sp. L-asparaginases: purification, characterization, and potential assessment as an antileukemic chemotherapeutic agent. Environ Sci Pollut Res. https://doi.org/10.1007/s11356-021-16175-5 - DOI
    1. Arumugam N, Thangavelu P (2022) Purification and anticancer activity of glutaminase and urease free intracellular l-asparaginase from Chaetomium sp. Protein Expr Purif 190:106006. https://doi.org/10.1016/j.pep.2021.106006 - DOI
    1. Ashok A, Doriya K, Rao JV, Qureshi A, Tiwari AK, Kumar DS (2019) Microbes producing L-asparaginase free of glutaminase and urease isolated from extreme locations of Antarctic soil and moss. Sci Rep 9:1423. https://doi.org/10.1038/s41598-018-38094-1 - DOI
    1. Beckett A, Gervais D (2019) What makes a good new therapeutic L-asparaginase? World J Microbiol Biotechnol 35:152. https://doi.org/10.1007/s11274-019-2731-9 - DOI

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