Extracellular L-asparaginase productive potential of the Priestia megaterium strain GB911 from Khanh Hoa sea of Viet Nam

Do Thi Phuong, Nguyen Mai Anh, Nguyen Thi Nga, Vu Thi Thu Huyen, Nguyen Thi Cuc, Trieu Ha Phuong, Le Thi Hong Minh, Do Thi Thao
Author affiliations

Authors

  • Do Thi Phuong Institute of Biotechnology, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Cau Giay, Ha Noi, Viet Nam
  • Nguyen Mai Anh Institute of Marine Biochemistry, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Cau Giay, Ha Noi, Viet Nam
  • Nguyen Thi Nga Institute of Biotechnology, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Cau Giay, Ha Noi, Viet Nam
  • Vu Thi Thu Huyen Institute of Marine Biochemistry, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Cau Giay, Ha Noi, Viet Nam
  • Nguyen Thi Cuc Institute of Biotechnology, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Cau Giay, Ha Noi, Viet Nam
  • Trieu Ha Phuong Institute of Biotechnology, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Cau Giay, Ha Noi, Viet Nam
  • Le Thi Hong Minh Institute of Marine Biochemistry, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Cau Giay, Ha Noi, Viet Nam
  • Do Thi Thao Institute of Biotechnology, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Cau Giay, Ha Noi, Viet Nam https://orcid.org/0000-0002-8760-264X

DOI:

https://doi.org/10.15625/2525-2518/17906

Keywords:

Priestia megaterium, L-asparaginase, cytotoxicity, extracellular enzyme, marine bacteria

Abstract

Currently, L-asparaginase isolated from terrestrial microorganisms has been employed for anticancer industrial production. This enzyme has the function of inhibiting the growth of acute lymphoblastic leukemia, Hodgkin's lymphomas and other cancers. In this study, for the first time, L-asparaginase (ASNase) productive capacity of forty marine bacteria originating from Khanh Hoa sea of Viet Nam was screened and reported. Among those, twenty eight isolates were clarified for their extracellular ASNase activity based on their ability to form a pink zone around colonies on asparagine agar plates. As a result, four strains GB910, GB911, GB976 and GB982 showed high secreted extracellular ASNase activity, ranging from 8.64 to 13.22 IU/mg. Among these four most potential strains, GB911 exhibited better enzyme production capacity and was subjected to taxonomy identification. According to the 16S rRNA gene sequence on the GenBank database, strain GB911 was identified as Priestia megaterium and registered in the GenBank database with accession number MW407014. The purified enzyme obtained from strain GB911 exhibited strong cytotoxic activity against five monolayer and suspension cancerous cell lines with IC50 values ranging from 39 mU/mL to 98 mU/mL. The strain could serve as a promising source for industrial production of ASNase for clinical chemotherapeutic treatment.

Downloads

Download data is not yet available.

References

Khalikova E., Susi P. and Korpela T. - Microbial dextran-hydrolyzing enzymes: fundamentals and applications, Microbiol. Mol. Biol. Rev. 69 (2005) 306-325. https://doi.org/10.1128/MMBR.69.2.306-325.2005.

Savitri N. A., Azmi W. - Microbial L-asparaginase: A potent antitumour enzyme, Indian J. Biotechnol. 2 (2003) 184-194.

Masetti R., Pession A. - First-line treatment of acute lymphoblastic leukemia with pegasparaginase, Biol.: Targets Ther. 3 (2009) 359. https://www.ncbi.nlm.nih.gov/ pmc/articles/PMC2726072/.

Cachumba J. J. M., Antunes F. A. F., Peres G. F. D., Brumano L. P., Santos J. C. D. and Silva S. S. D. -Current applications and different approaches for microbial L-asparaginase production, Braz. J. Microbiol. 47 (1) (2016) 77-85. https://doi.org/10.1016/ j.bjm.2016.10.004.

Avramis V. I., Tiwari P. N. - Asparaginase (native ASNase or pegylated ASNase) in the treatment of acute lymphoblastic leukemia, Int. J. Nanomed 1(3) (2006) 241. https://pubmed. ncbi.nlm.nih.gov/17717965/.

Imhoff J. F., Labes A. and Wiese J. - Bio-mining the microbial treasures of the ocean: new natural products, Biotechnol. Adv. 29 (5) (2011) 468-482. https://doi.org/10.1016/ j.biotechadv.2011.03.001.

Gulati R., Saxena R. and Gupta R. - A rapid plate assay for screening l‐asparaginase producing micro‐organisms, Lett. Appl. Microbiol. 24 (1) (1997) 23-26. https://doi.org/10.1046/j.1472-765X.1997.00331.x.

Alrumman S., Mostafa Y., Al-Izran K. A., Alfaifi M., Taha T. and Elbehairi S. -Production and anticancer activity of an L-asparaginase from Bacillus licheniformis isolated from the Red Sea, Saudi Arabia, Sci. Rep. 9 (2019) 1-14. https://doi.org/10.1038/s41598-019-40512-x.

Do T. T., Do T. P., Nguyen T. N., Nguyen T. C., Vu T. T. P. and Nguyen T. G. A. - Nanoliposomal L-asparaginase and its antitumor activities in Lewis lung carcinoma tumor-induced BALB/c mice, Adv. Mater Sci. Eng. Special issue 1 (2019) 1-8. doi:10.1155/2019/3534807. https://doi.org/10.1155/2019/3534807.

Wriston J. C. - Asparaginase, Methods Enzymol. 13 (1985) 608-18. https://doi.org/ 10.1016/0076-6879(71)17273-4.

Ameen F., Alshehri W. A., Al-Enazi N. M. and Almansob A. - L-Asparaginase activity analysis, ansZ gene identification and anticancer activity of a new Bacillus subtilis isolated from sponges of the Red Sea, Biosci. Biotech. Biochem 84 (2020) 2576-2584. https://doi.org/10.1080/09168451.2020.1807310.

Izadpanah Qeshmi F., Javadpour S., Malekzadeh K., Tamadoni Jahromi S. and Rahimzadeh M. - Persiangulf is a bioresource of potent L-asparaginase producing bacteria: Isolation & molecular differentiating, Int. J. Environ. Res. 8 (3) (2014) 813-818. https://doi.org/10.22059/IJER.2014.774

Moushree P. R., Vaskar D. and Amal P. - Isolation, purification and characterization of an extracellular L-asparaginaseproduced by a newly isolated Bacillus megaterium strain MG1from the water bodies of Moraghat forest, Jalpaiguri, India, J. Gen. Appl. Microbiol., 65 (3)(2019): 137-144. https://doi.org/ 10.2323/jgam.2018.07.004.

Michalska K., Jaskolski M. - Structural aspects of L-asparaginases, their friends and relations. Acta.Biochim. Pol. 53 (4) (2006) 627-640. https://pubmed.ncbi. nlm.nih.gov/17143335/

Pal Roy M., Mazumdar D., Dutta S., Saha S. P. and Ghosh S. - Cloning and expression of phytase appA gene from Shigella sp. CD2 in Pichia pastoris and comparison of properties with recombinant enzyme expressed in E. coli, PloS one 11 (1) (2016) e0145745. https://doi.org/10.1371/journal.pone.0145745.

Mohapatra B., Sani R. and Banerjee U. - Characterization of L‐asparaginase from Bacillus sp. isolated from an intertidal marine alga (Sargassum sp.), Lett. Appl. Microbiol. 21 (6) (1995): 380-383. https://doi.org/10.1111/j.1472-765X.1995.tb01086.x.

Sunitha M., Ellaiah P. and Devi R.B. - Screening and optimization of nutrients for L-asparaginase production by Bacillus cereus MNTG-7 in SmF by plackett-burmann design, Afr. J. Microbiol. Res. 4 (4) (2010) 297-303. https://doi.org/ 10.5897/AJMR.9000639.

Vidhya M., Aishwarya R., Alagarsamy S. and Rajesh T.S. - Production, purification and characterisation of extracellular L-asparaginase from a soil isolate of Bacillus sp. Afr. J. Microbiol. Res. 4 (560) (2010) 1862-1867.

Jia M., Xu M., He B. and Rao Z. - Cloning, expression, and characterization of L-asparaginase from a newly isolated Bacillus subtilis B11–06, J. Agric. Food Chem. 61 (39) (2013) 9428-9434. https://doi.org/10.1021/jf402636w.

Mesas J. M., Gil J. A. and Martn J. F. - Characterization and partial purification of L-asparaginase from Corynebacterium glutamicum, Microbiology 136 (3) (1990) 515-519. https://pubmed.ncbi.nlm.nih.gov/2391490/.

Singh Y., Gundampati R. K., Jagannadham M. V. and Srivastava S. - Extracellular L-asparaginase from a protease-deficient Bacillus aryabhattai ITBHU02: purification, biochemical characterization, and evaluation of antineoplastic activity in vitro, Appl. Biochem. Biotechnol.171 (2013) 1759-1774. https://doi.org/10.1007/s12010-013-0455-0.

Roy M. P., Das V. and Patra A. - Isolation, purification and characterization of an extracellular L-asparaginase produced by a newly isolated Bacillus megaterium strain MG1 from the water bodies of Moraghat forest, Jalpaiguri, India, J. Gen. Appl. Microbiol. 65 (3) (2019) 137-144. https://doi.org/10.2323/jgam.2018.07.004.

Kumar DS, Sobha K. - L-asparaginase from microbes: a comprehensive review, Adv. Biores. 3 (2012) 137- 157.http://soeagra.com/abr/abrdec 2012/22.pdf.

Bhat M., Marar T. - Cytotoxic Effect of Purified L-asparaginase from Salinicoccus sp. M KJ997975, Int. J. Curr. Microbiol. App. Sci. 4(4) (2015) 701-712

Aljewari H. S., Nader M. I. and Alfaisal A. H. M. - High efficiency, selectivity against cancer cell line of purified L-asparaginase from pathogenic Escherichia coli, Int. J. Pharm. Pharm. Sci. 4 (2010) 199-204.

Mahajan R. V., Kumar V., Rajendran V., Saran S., Ghosh P. C. and Saxena R. K. - Purification and characterization of a novel and robust L-asparaginase having low-glutaminase activity from Bacillus licheniformis: in vitro evaluation of anti-cancerous properties, PloS One 9 (6) (2014), e99037. https://doi.org/10.1371/journal.pone.0099037.

Tardito S., Uggeri J., Bozzetti C., Bianchi M., Rotoli B., Franchi-Gazzola R., Gazzola G., Gatti R. and Bussolati O. - The inhibition of glutamine synthetase sensitizes human sarcoma cells to L-asparaginase. Cancer Chemother.Pharmacol.60 (2007) 751-758. https://doi.org/10.1007/s00280-007-0421-z.

Cappelletti D., Chiarelli L. R., Pasquetto M. V., Stivala S., Valentini G. and Scotti C. -Helicobacter pyloril-asparaginase: a promising chemotherapeutic agent, Biochem. Biophys. Res. Commun. 377(4) (2008) 1222-1226. https://doi.org/10.1016/ j.bbrc.2008.10.118.

Downloads

Published

23-02-2024

How to Cite

[1]
D. T. Phuong, “Extracellular L-asparaginase productive potential of the Priestia megaterium strain GB911 from Khanh Hoa sea of Viet Nam”, Vietnam J. Sci. Technol., vol. 62, no. 1, pp. 35–47, Feb. 2024.

Issue

Section

Natural Products

Most read articles by the same author(s)

<< < 1 2