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L-Asparaginase producing bacteria were isolated from soil samples under optimum conditions using submerged fermentation. Their abilities to produce asparaginase at different pH, temperature, incubation temperature, utilization of different carbon and nitrogen sources as well as their specific conditions for optimal activity were also investigated. Streptococcus spp. D1, Bacillus polymyxa and Streptococcus spp. D2 showed optimum asparaginase production at pH 8 with activities of 11.6 U/ml, 8.8 U/ml and 7.9 U/ml respectively. The pH 7 was observed as optimum pH for Bacillus firmus (8.8 U/ml) while optimum pH 6 was observed for Bacillus circulans and Paenibacillus validus. Maximum L-asparaginase productivity was attained at a temperature of 45°Cby Bacillus firmus, Streptococcus sp. D1 and Bacillus circulans with activity of 4.6 U/ml, 5.6 U/ml and 3.8 U/ml respectively while 35°C incubation temperature was optimum for Paenibacillus validus and Bacillus polymyxa with enzyme activity of 6.2 U/ml and 6.1 U/ml respectively. Mannitol supported the maximum asparaginase production of Bacillus circulans, Streptococcus sp. D2 and Bacillus polymyxa while maltose was observed as the best carbon source for Streptococcus sp. D1 and Bacillus firmus; and sucrose for Paenibacillus validus. The optimum nitrogen source was casein for Bacillus circulans (7.57 U/ml) and Streptococcus spp. D1 (6.19 U/ml), Yeast extract for Bacillus polymyxa (7.037 U/ml)and Bacillus firmus(5.368 U/ml) while NaNO3 supported optimum L-asparaginase production for Streptococcus sp. D2 (6.006 U/ml) and Paenibacillus validus (4.754 U/ml). At optimum conditions, Bacillus polymyxa had the highest (4.835 U/ml) while Bacillus circulans had the least (2.981 U/ml) asparaginase activity. In all, the bacterial isolates prefers slightly alkaline to alkaline medium (pH 6-8) for optimum asparaginase production.
References
Fernandes AI, Gregoriadis G. Polysialylated asparaginase: preparation, activity and pharmacokinetics. Biochim Biophys Acta 1997; 1341: 26-34. http://dx.doi.org/10.1016/S0167-4838(97)00056-3
Muthusivaramapandian M, Arrivukkarasan S, Aravindan R, Viruthagiri T. Perspectives and Applications of anticancer enzyme L- asparaginase. Asian J Microbiol Biotechnol Environ Sci 2008; 10(4): 851-854.
Cammack KA, Marlborough DI, Miller DS. Physical properties and subunit structure of L-asparaginase isolated from Erwinia carotovora. J Biochem 1972; 126: 361-379.
Manna S, Sinaha A, Sadhukhan R, Chakrabarty SL. Purification, characterization and antitumor activity of L-asparaginase isolated from Pseudomonas stutzeri. MB-405. Cur Microbiol 1995; 30: 291-298. http://dx.doi.org/10.1007/BF00295504
Abdel-Fatteh Y, Olama ZA. L-asparaginase produced by Pseudomonas aeruginosa in solid state culture: evaluation and optimization of culture conditions using factorial designs. Process Biochem 2002; 38: 115-122. http://dx.doi.org/10.1016/S0032-9592(02)00067-5
Qin M, Zhao F. L-asparaginase release from Escherichia coli cells with aqueous two-phase micellar systems. Appl Biochem Biotechnol 2003; 110(1): 11-21. http://dx.doi.org/10.1385/ABAB:110:1:11
Bansal S, Gnaneswari P, Mishra P, Kundu B. Structural stability and functional analysis of L-asparaginase from Pyrococcus furiosus. Biochem 2010; 75(3): 375-381.
Duval M, Suciu S, Ferster A, Rialland X, Nelken B, Lutz P, Benoit Y, et al. Comparison of Escherichia coli Asparaginase with Erwinia asparaginase in the treatment of childhood lymphoid malignancies. Results of a randomized European organization for research and treatment of cancer-children’s leukemia group phase 3 trails. Blood 2002; 99: 2734-2739. http://dx.doi.org/10.1182/blood.V99.8.2734
Hosamani R, Kaliwal BB. L-asparaginase an anti-tumor agent production by Fusarium equiseti using solid state fermentation. Inter J Drug Discovery 2011; 3(2): 88-99.
Pieters R, Hunger SP, Boos J, Rizzari C, Silverman L, Baruchel A, Goekbuget N, Schrappe M, Ching-Hon Pui. Cancer 2011; 117(2): 238-249. http://dx.doi.org/10.1002/cncr.25489
Verma N, Kumar K, Kaur G, Anand S. Escherichia coli K-12 asparaginase-based asparagine biosensor for leukemia. Artif. Cells Blood Substit. Immobilization Biotechnol 2007; 35: 449-456. http://dx.doi.org/10.1080/10731190701460358
Prakasham RS, Hymavathi M, Subba RC, Arepalli SK, Venkateswara RJ, Kavin KP, Nasaruddin K., et al. Evaluation of antineoplastic activity of extracellular asparaginase produced by isolated Bacillus circulans. Appl Biochem Biotechnol 2010; 160: 72-80. http://dx.doi.org/10.1007/s12010-009-8679-8
Shah AJ, Karadi RV, Parekh PP. Isolation, optimization and production of L-asparaginase from coliform bacteria. Asian J Biotechnol 2010; 2: 169-177. http://dx.doi.org/10.3923/ajbkr.2010.169.177
Imada A, Igarasi S, Nakahama K, Isono M. Asparaginase and glutaminase activities of microorganisms. J Gen Microbiol 1973; 76: 85-89. http://dx.doi.org/10.1099/00221287-76-1-85
Gulati R, Saxena RK, Gupta RA. Rapid Plate Assay for Screening L-Asparaginase Producing Micro organisms. Lett Appl Microbiol 1997; 24: 23-26. http://dx.doi.org/10.1046/j.1472-765X.1997.00331.x
Kamble KD, Khade PJ. Studies on antineoplastic enzyme producing bacteria from soil. Inter J Pharmaceut Biomed Res 2012; 2: 94-99.
Narayana K. L-asparaginase production by Streptomyces albidoflavus. Indian J Microbiol 2007; 48(3): 331-336. http://dx.doi.org/10.1007/s12088-008-0018-1
Borkotaky B, Bezbaruah RL. Production and properties of asparaginase from a new Erwinia sp. Folia Microbiol 2002; 47: 473-476. http://dx.doi.org/10.1007/BF02818783
Dhevagi P, Poorani E. Isolation and characterization of L-asparaginase from marine actinomycetes. Indian J Biotechnol 2006; 5: 514–520.
Thaer TA, Ellaiah P. L-asparaginase production by Streptomycete and optimization of production parameters. J Pharmaceut Biomed Sci 2013; 29: 859-869.
Praveen K, Thangabalan B, Venkata R, Vadivel MK, Manohar BS, Srinivasa D. Optimization of parameters for the production of L-asparaginase by Serratia marcescens. J Pharmaceut Biomed Sci 2011; 7: 20.
Susmita S, Mandal SK. Production purification and characterization of extracellular Anti-leukaemic L-asparaginase from isolated Bacillus subtilis using Solid state fermentation. Inter J Appl Biol Pharmaceut Technol 2013; 4(3): 89-99.
Soniyamby AR, Lalitha S, Praveesh BV, Priyadarshini V. Isolation, production and anti-tumour activity of L-asparaginase of Penicillium sp. Inter J Microbiol Res 2011; 2(1): 38-42.
Amena S, Vishalakshi N, Prabhakar M, Dayanand A, Lingappa K. Production, purification and characterization of L-asparaginase from Streptomyces gulbargensis. Brazilian J Microbiol 2010; 41: 173- 178. http://dx.doi.org/10.1590/S1517-83822010000100025
Deokar VD, Vetal MD, Rodrigues L. Production of intracellular L-asparaginase from Erwinia carotovora and its statistical optimization using response surface methodology (RSM). Inter J Chem Sci Applic 2010; 1: 25-36.
Kenari SLD, Alemzadeh I, Maghsodi V. Production of L-asparaginase from Escherichia coli ATCC 11303: Optimization by response surface methodology. Food Bioproduction Process 2011; 86: 315-321. http://dx.doi.org/10.1016/j.fbp.2010.11.002
Savitri NA, Azmi W. Microbial L-asparaginase: A potent antitumour enzyme. Indian J Biotechnol 2003; 2: 184-194
Liu FS, Zajic JE. L-asparaginase Synthesis by Erwinia aroideae. Appl Microbiol 1972; 33: 667-668.
Verma N. L-asparaginase: a promising chemotherapeutic agent. Crit Rev Biotechnol 2007; 27: 45-62. http://dx.doi.org/10.1080/07388550601173926
Singh Y, Srivastava SK. Screening and characterization of microorganisms capable of producing antineoplastic drug, L-asparaginase. Inter J Biol Med Res 2012; 3(4): 2548-2554.
Makky EA, Jee-Jian O, Md-Rezaul K, Lee CM. Production and optimization of L-asparaginase by Bacillus sp. KK2S4 from corn cob. Afr J Biotech 2013; 12(9): 2654-2658.
Kavitha A, Vijayalakshmi M. A study on L- asparaginase of Nocardia levis MK-VL-113. Scientific World Journal 2012; 2012: 1-5. http://dx.doi.org/10.1100/2012/160434
Narayana KJP, Kumar KG, Vijayalakshmi, M. 2008. L-Asparaginase production by Streptomyces albidoflavus. Indian J Microbiol 48(3): 331-336. http://dx.doi.org/10.1007/s12088-008-0018-1
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