{"references": ["1. Hwang HJ, Kim EH, Cho YD. Isolation and properties of arginase from a shade plant, ginseng (Panax ginseng CAMeyer) roots. Pytochemistry. 2001; 1015-1024.", "2. Zhang X, Zhang X, Takano T, Liu S, Bu Y. The Research Progress of Plant Arginase and the Roles in Stresses. Cell Biology and Biophysics. 2014; 3 (1)1-6.", "3. El-Sayed, Shindia AA, Diab AA, Rady AM. Purification and immobilization of L-arginase from thermotolerant Penicillium chrysogenum KJ185377.1 with unique kinetic properties as thermostable anticancer enzyme. Arch Pharm Res. 2014 DOI 10.1007/s12272-014-0498-y.", "4. Dzikowska JP, Le-Caer P, Jonczyk P, Weglenski P. Purification of arginase from Aspergillus nidulans, Acta Biochim Pol. 1994; 467-471", "5. Bascaran, V., Haridsson, C. and Bran, A.F. Regulation of nitrogen catabolic enzymes in Streptomyces calvuligerus. J. Gen. Microbial. 1989;135(9): 2465- 2474.", "6. Zhang X, Zhang C, Wu D, Lu G, Guo X, Mao Y, Zhang D, Wang D, Li D, Zou Q. Expression, purification and characterization of arginase from Helicobacter pylori in its apo form. PLoS ONE. 2011, 6:e26205", "7. Wang Z, Shi Y, Li Y, Zeng X, Fan J, Sun Y, Xian Z, Zhang G, Wang S, Hu H, Ju D. Involvement of autophagy in recombinant human arginase- induced cell apoptosis and growth inhibition of malignant melanoma cells. Appl Microbiol Biotechnol. 2014, 98: 2485-2494", "8. Adinarayana K, Ellaiah P. Investigations on alkaline protease production with B. Subtilis PE-11 Immobilised in calcium alginate gel beads. Process Biochem. 2004;39:1331-1339", "9. Lee KY, Mooney DJ. Alginate: properties and biomedical applications. Progress in polymer science. 2012; 37(1):106-126", "10. Karacaoglu S, Timur S, Telefoncu A. Artificial cells, blood substitutes and immobilization. Biotechnol. 2003;31 (3): 357-363.", "11. Mcgee D.J, Zabaleta J, Viator R.J, Testrman T.L. Ochoa A.C, Mendz G.L. Purification and characterization of Helicobactor pylori arginase, RocF: Unique features among The arginase super family. Eur J Biochem. 2004; 271: 1952-1962", "12. Bickerstaff GF. Immobilization of enzymes and cells: Some practical considerations. In: Bickerstaff GF,ED. Immobilization of enzymes and cells. Totowa, NJ: Humana Press; 1997;1-12", "13. Bolivar J.M, Wilson L, Ferrarotti S.A, Guis an J.S, Ferm andez-Lafuente, Mateo C. Improvement of the stability of alcohol dehydrogenase by covelent immobilization on glyoxyl-agarose. J Biotechnology. 2006;125(1):85-94.", "14. Beshav U, Abd-EI-Haleem D, Moawad H, Zaki S. Phenol biodegradation by free and immobilized Acinetobactor. Biotechnol Lett. 2002;24:1295-1297.", "15. Orive G, Carcaboso AM, Hern\u00e1ndez RM, Gasc\u00f3n AR, Pedraz JL. Biocompatibility evaluation of different alginates and alginate-based microcapsules. Biomacromolecules. 2005 ;6(2):927-31.", "16. Brady D, Jordaan J. Advances in enzyme immobilization. Biotechnology Letters, 2009;31(11): 1639-1650", "17. Guzik U, Kocurek KH, Krysiak M, and Nska W D. Degradation potential of protocatechuate 3,4- dioxygenase from crude extract of stenotrophomonas maltophilia Strain KB2 Immobilized in calcium alginate hydrogels and on glyoxyl agarose. Biomed Research International. 2014;8.", "18. Lee J, Lee KY. Local and sustained vascular endothelial growth factor delivery for angiogenesis using an injectable system. Pharm Res. 2009; 26:1739\u20131744", "19. Arica B, Calis S, Kas HS, Sargon MF. Hincal AA 5- flurouracil encapsulated alginate beads for the treatment of breast cancer. Int J Pharmaceut. 2002;242- 267.", "20. Guisan JM. Immobilization of enzymes and cells. New York, Humana Press, 2006", "21. Gombotz WR, Wee SF. Protein release from alginate matrices.Adv Drug Deliv Rev 1998; 31: 267-285."]}

Multiple applicability of therapeutic potential obtained from L-arginase, especially highly purified ones, is being widely appreciated these days in scientific fields. Due to lesser physiological stability and its non acceptance in human body due to allergic reactions, its use is however hampered. Hence, this study, while hypothesizing that enabling entrapment of Larginase in adequate matrix may be biologically acceptable, aimed to immobilise the L-rginase produced by Actinomycete and to assess its stability at varied pH, temperature and in serum under conditions. The alginate beads formed herein in vitro were of uniform size (4.00 mm in external diameter) and have shown entrapment efficiency of 84.23±0.63 %.The stability of entrapped L-arginase at different pH and temperature was found to be significantly increased/ high (p value 0.001). The enzyme retained its cent percent activity even after 5 hours of preincubation of alginate beads under spectrum of conditions. No loss in activity of L-arginase occurred upon its incubation in commercially available fetal bovine serum. This study hence opens vistas of further research opportunities in alleviation of suffering of cancer patients as alginate entrapment has proven longer bioavailability and hence greater efficiency cum effectiveness of L-arginase herein as anticancer agent.