Isolation and Preliminary Characterization of L-Asparaginase-Producing Bacteria from Marine Sponges Collected in the Makassar Sea
Abstract
This study provides an initial exploration aimed at discovering new sources of L-asparaginase from marine sponge-associated bacteria, representing a novelty due to the limited reports from the Makassar Sea ecosystem. The research addresses the need for alternative L-asparaginase producers with improved therapeutic potential and biological compatibility by isolating candidate bacteria from marine sponges. Isolation was performed using M9 and Asparagine Glucose Salt Agar to detect bacteria capable of hydrolyzing L-asparagine, indicated by the formation of pink halo zones. Three isolates (C6, B18, KH6) exhibiting the strongest responses were selected for further enzymatic evaluation using the Nessler method. The results revealed that isolate C6 displayed the highest activity (74.89 IU/mL), followed by B18 (58.44 IU/mL), whereas KH6 showed low activity (9.57 IU/mL). These findings demonstrate that marine sponges represent a promising reservoir of novel L-asparaginase-producing bacteria, with isolate C6 emerging as the most promising candidate for future purification and biochemical characterization. This study provides an important basis for developing alternative L-asparaginase sources for biotechnological applications.
Keywords:
enzymatic activity, L-asparaginase, marine bacteria, marine sponge
References
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[2] S. Rajan and B. Deivasigamani, “Screening, Production and Characterization of extracellular glutaminase free L-Asparaginase producing endo-symbiontic bacteria from the gut of Mugil cephalus (Mullet fish),” Asian J Pharm Pharmacol, vol. 4, no. 3, pp. 288–292, 2018, doi: 10.31024/ajpp.2018.4.3.8.
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[12] K. Tsegaye, B. A. Tsehai, and B. Getie, “Desirable L-asparaginases for treating cancer and current research trends,” Front Microbiol, vol. 15, Mar. 2024, doi: 10.3389/fmicb.2024.1269282.
[13] M. Van Trimpont et al., “Novel Insights on the Use of L-Asparaginase as an Efficient and Safe Anti-Cancer Therapy,” Cancers (Basel), vol. 14, no. 4, p. 902, Feb. 2022, doi: 10.3390/cancers14040902.
[14] S. A. Alrumman, Y. S. Mostafa, K. A. Al-izran, M. Y. Alfaifi, T. H. Taha, and S. E. Elbehairi, “Production and Anticancer Activity of an L-Asparaginase from Bacillus licheniformis Isolated from the Red Sea, Saudi Arabia,” Sci Rep, vol. 9, no. 1, Dec. 2019, doi: 10.1038/s41598-019-40512-x.
[15] P. Shirazian, S. Asad, and M. A. Amoozegar, “The potential of halophilic and halotolerant bacteria for the production of antineoplastic enzymes: L-asparaginase and L-glutaminase.,” EXCLI J, vol. 15, pp. 268–79, 2016, doi: 10.17179/excli2016-146.
[16] W. Bakeer, M. Amer, W. G. Hozayen, N. S. Kotb, and M. H. A. Hassan, “Isolation of asparaginase-producing microorganisms and evaluation of the enzymatic antitumor activity,” Egyptian Pharmaceutical Journal, vol. 21, no. 3, pp. 282–292, Jul. 2022, doi: 10.4103/epj.epj_11_22.
[17] D. E. Mathew, A. Soni, P. B. Shinde, and V. A. Mantri, “A Potent Drug l-Asparaginase from Marine Origins: A Comprehensive Review,” in Marine Bioactive Molecules for Biomedical and Pharmacotherapeutic Applications, Singapore: Springer Nature Singapore, 2023, pp. 141–159. doi: 10.1007/978-981-99-6770-4_8.
[18] Herwin et al., “Molecular Analysis And Bioactive Compounds Of Endophytic Fungus IFATL-05 Isolate From Helminthostashys Zeylanica Linn. Roots As Antibacterial,” IOSR Journal Of Pharmacy And Biological Sciences (IOSR-JPBS) e-ISSN, vol. 20, no. 1, pp. 61–68, 2025, doi: 10.9790/3008-2001016168.
[19] C. Ramesh, B. R. Tulasi, M. Raju, N. Thakur, and L. Dufossé, “Marine Natural Products from Tunicates and Their Associated Microbes,” Mar Drugs, vol. 19, no. 6, p. 308, May 2021, doi: 10.3390/md19060308.
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[22] N. Chakravarty, Priyanka, J. Singh, and R. P. Singh, “A potential type-II L-asparaginase from marine isolate Bacillus australimaris NJB19: Statistical optimization, in silico analysis and structural modeling,” Int J Biol Macromol, vol. 174, pp. 527–539, Mar. 2021, doi: 10.1016/j.ijbiomac.2021.01.130.
[23] W.-J. Yu et al., “The Characterization of L-Asparaginase with Low L-Glutaminase Activity Produced by the Marine Pseudomonas sp. Strain GH-W2b,” Microbiol Res (Pavia), vol. 16, no. 1, p. 2, Dec. 2024, doi: 10.3390/microbiolres16010002.
[24] W. A. Mohammed Hadi, B. T. Edwin, and A. Jayakumaran Nair, “Isolation and identification of marine Bacillus altitudinis KB1 from coastal Kerala: asparaginase producer,” Journal of the Marine Biological Association of India, vol. 63, no. 2, pp. 43–48, Jan. 2021, doi: 10.6024/jmbai.2021.63.2.2195-06.
[25] W. Bakeer, M. Amer, W. G. Hozayen, N. S. Kotb, and M. H. A. Hassan, “Isolation of asparaginase-producing microorganisms and evaluation of the enzymatic antitumor activity,” Egyptian Pharmaceutical Journal, vol. 21, no. 3, pp. 282–292, Jul. 2022, doi: 10.4103/epj.epj_11_22.
[26] M. Muzuni, J. Jamaluddin, S. Suriana, A. Ardiansyah, and N. A. Yanti, “Skrining Bakteri Termohalofilik Penghasil L-asparaginase dari Sumber Air Panas Wawolesea Sulawesi Tenggara dan Uji Aktivitas Enzimnya,” ALCHEMY Jurnal Penelitian Kimia, vol. 20, no. 1, p. 12, Mar. 2024, doi: 10.20961/alchemy.20.1.73523.12-21.
[27] A. Badoei-Dalfard, “L-asparaginase Production by Pseudomonas pseudoalcaligenes Strain JHS-71 Isolated from Jooshan Hot Spring,” Mol Biol Res Commun, vol. 5, no. 1, pp. 1–10, Mar. 2016.
[28] U. R. Abdelmohsen et al., “Isolation, Phylogenetic Analysis and Anti-infective Activity Screening of Marine Sponge-Associated Actinomycetes,” Mar Drugs, vol. 8, no. 3, pp. 399–412, Feb. 2010, doi: 10.3390/md8030399.
[29] S. Miyauchi et al., “Visual Comparative Omics of Fungi for Plant Biomass Deconstruction,” Front Microbiol, vol. 7, Aug. 2016, doi: 10.3389/fmicb.2016.01335.
[30] G. D’Souza et al., “Cell Aggregation Is Associated with Enzyme Secretion Strategies in Marine Polysaccharide-Degrading Bacteria,” ISME J, vol. 17, no. 5, pp. 703–711, May 2023, doi: 10.1038/s41396-023-01385-1.
[31] N. Lefin et al., “Current State of Molecular and Metabolic Strategies for the Improvement of L-Asparaginase Expression in Heterologous Systems,” Front Pharmacol, vol. 14, Jun. 2023, doi: 10.3389/fphar.2023.1208277.
[32] M. R. Bhat, J. S. Nair, and T. Marar, “Isolation and Identification of L-Asparaginase Producing Salinicoccus sp. M KJ997975 from Soil Microbial Flora,” Int J Pharm Sci Res, vol. 6, no. 8, p. 3599, 2015, doi: 10.13040/IJPSR.0975-8232.6(8).3599-05.
[33] W. A. Mohammed Hadi, B. T. Edwin, and A. Jayakumaran Nair, “Isolation and Identification of Marine Bacillus altitudinis KB1 from Coastal Kerala: Asparaginase Producer,” Journal of the Marine Biological Association of India. Marine Biological Association of India, vol. 63, no. 2, pp. 43–48, 2021, doi: 10.6024/jmbai.2021.63.2.2195-06.
[34] G. M. Al-Harbi et al., “Isolation and Characterization of L-Asparaginase-Producing Bacteria from the Arabian–Persian Gulf Region: First Report on Bacillus xiamenensis ASP-J1-4 as a Producer and Its Potential Application,” Mar Drugs, vol. 23, no. 5, p. 194, Apr. 2025, doi: 10.3390/md23050194.
[35] V. P. Lailaja, T. G. Sumithra, S. R. K. Sharma, M. A. Mohammed, U. Sivan, and V. N. Anusree, “Tapping the untapped: type II L-asparaginase from marine crustacean-derived Chryseomicrobium amylolyticum as a potential bio better for blood cancer therapy,” Sci Rep, vol. 15, no. 1, Dec. 2025, doi: 10.1038/s41598-025-08962-8.
[36] B. Meena et al., “Molecular Expression of L-Asparaginase Gene from Nocardiopsis alba NIOT-VKMA08 in Escherichia coli: A Prospective Recombinant Enzyme for Leukaemia Chemotherapy,” Gene, vol. 590, no. 2, pp. 220–226, Sep. 2016, doi: 10.1016/j.gene.2016.05.003.
[37] D. E. Mathew, S. A. Siddiqui, A. Soni, A. K. Vala, P. B. Shinde, and V. A. Mantri, “Glutaminase-Free L-Asparaginase from Seaweed-Associated Bacillus licheniformis with Promising Therapeutic Potential,” Discover Oceans, vol. 2, no. 1, p. 53, Oct. 2025, doi: 10.1007/s44289-025-00089-y.
Published
2026-05-31
Section
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