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Journal of Pharmaceutical Research

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Purification and Characterization of L-Arginine Deiminase from Vibrio Alginolyticus 1374
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Journal of Pharmaceutical Research

DOI: 10.18579/jpcrkc/2016/15/1/93748

Year: 2016, Volume: 15, Issue: 1, Pages: 20-25

Original Article

Purification and Characterization of L-Arginine Deiminase from Vibrio Alginolyticus 1374

Rahamat Unissa 1*, Muhammad Sudhakar 1, A. Sunil Kumar Reddy 2
  • Department of Pharmaceutical Biotechnology, Malla Reddy College of Pharmacy, Maisammaguda, Dhulapally, Secunderabad, Osmania University, Telangana, India
  • Department of Pharmaceutical Chemistry, Bharat Institute of Technology Pharmacy, Jawaharlal Technological University of Hyderabad, Ibrahimpatnam, Hyderabad, Telangana, India
Creative Commons License

This work is licensed under a Creative Commons Attribution 4.0 International License.

Abstract

Aim: The aim of our present study was to purify and characterize l-arginine deiminase isolated from marine Vibrio alginolyticus1374.Methodology: Arginine deiminase (AD), an arginine-degrading enzyme, has been used in the treatment of tumours, sensitive to arginine deprivation, such as malignant melanoma and hepatocellular carcinoma. Proteins of microbial origin are always associated with mild to severe hypersensitivities. Moreover, proteins from terrestrial sources were found to exhibit stability problems at physiological environment. Hence considering the fact that the characteristics of the enzyme depends upon sources from which it has been isolated, we have use marine organism for the present study expecting to yield therapeutically and physiologically stable enzyme. ADI production was carried out under optimal conditions by shake flask method. The enzyme thus obtained was purified by ammonium sulphate fractionation, ion exchange and gel permeation chromatography. The purity of the enzyme was further confirmed by sodium dodecyl sulphate polyacrylamide gel electrophoresis, and it was characterized to know its properties.Results: It was active at physiological pH, showed high substrate specificity towards l-arginine. It also exhibited high salt and temperature tolerance indicating good scope for its industrial and therapeutic applications.Conclusions: ADI obtained from Vibrio alginolyticus 1374 can be a good candidate for the treatment of human cancers.

References

  • Chowdary MAR, Yamanaka H, Miyoshi S. Ecology and seasonal distribution of Vibrio parahaemolyticus in aquatic environments of a temperate region. FEMS MicrobiolEcol.1990; 74:1-110.

  • Zanetti S, Deriu A, Volterra L. Virulence factors in Vibrio alginolyticus strains isolated from aquatic environments. Ann Ig2000;12(6): 487 � 491.

  • Pezzlo M, Valter PJ, Burns MJ. Wound infection associated with Vibrio alginolyticus. Am J Clin Pathol. 1979;71(4):476-8.

  • A. Casiano-Colon, R.E. Marquis, Role of the arginine deiminase system in protecting oral bacteria and an enzymatic basis for acid tolerance, Appl. Environ. Microbiol. 1988; 54: 1318�1324.

  • B.A. Degnan, M.C. Fontaine, A.H. Doebereiner, J.J. Lee, P. Mastroeni, G. Dougan, J.A. Goodacre, M.A. Kehoe. Characterization of an isogenic mutant of Streptococcus pyogenes Manfredo lacking the ability to make streptococcal acid glycoprotein, Infect. Immun.2000; 68: 2441�2448.

  • Nada Z. Mahdy1, Shatha S. Al-Tahan, Nahi Y. Yaseen .Optimization of ArginineDeiminase production from a local higher productive isolate Enterococcus faecium M1.Iraqi Journal of Cancer and Medical Genetics, 2014; 7-1.

  • Das K, Butler GH, Kwiatkowski V, Clark AD Jr, Yadav P, Arnold E. Crystal structures of arginine deiminase with covalent reaction intermediates; implications for catalytic mechanism. Structure, 2004; 12(4): 657�667.

  • T. Bauchop, The growth of micro-organisms in relation to their energy supply, J. Gen. Microbiol. 1960; 23: 457�469.

  • Shibatani T, Kakimoto T, Chibata I Crystallization and properties of L-arginine deiminase of Pseudomonas putida. J BiolChem1975; 250(12):4580-4583.

  • H.H. Moustafa, E.B. Collins, Molar growth yields of certain lactic acid bacteriaas influenced by autolysis, J. Bacteriol.1968; 96 : 117�125.

  • S. Jonsson, E. Clausen, J. Raa, Amino acid degradation by a Lactobacillusplantarum strain from fish, Syst. Appl. Microbiol. 1983; 4:148�154.

  • V.L. Crow, T.D. Thomas, Arginine metabolism in lactic streptococci, J. Bacteriol.1982;150: 1024�1032.

  • G.G. Gonzalez, C.V. Byus, Effect of dietary arginine restriction upon ornithineand polyamine metabolism during two-stage epidermal carcinogenesis in themouse, Cancer Res. 1991; 51 : 2932�2939.

  • B.J. Dillon, V.G. Prieto, S.A. Curley, C.M. Ensor, F.W. Holtsberg, J.S. Bomalaski, M.A. Clark, Incidence and distribution of argininosuccinate synthetase deficiency in human cancers: a method for identifying cancers sensitive to arginine deprivation, Cancer 2004; 100;826�833.

  • B.J. Dillon, F.W. Holtsberg, C.M. Ensor, J.S. Bomalaski, M.A. Clark, Biochemical Characterization of the arginine degrading enzymes arginase and argininedeiminase and their effect on nitric oxide production, Med. Sci. Monitor 2002: BR248�BR253.

  • K. Miyazaki, H. Takaku, M. Umeda, T. Fujita, W.D. Huang, T. Kimura, J.Yamashita, T. Horio, Potent growth inhibition of human tumor cells in cultureby arginine deiminase purified from a culture medium of a Mycoplasmainfectedcell line, Cancer Res. 1990;50 : 4522�4527.

  • R. Philip, E. Campbell, D.N. Wheatley, Arginine deprivation, growth inhibitionand tumour cell death: 2. Enzymatic degradation of arginine in normal and malignant cell cultures, Br. J. Cancer 2003; 88:613�623.

  • H. Terayama, T. Koji, M. Kontani, T. Okumoto, Arginase as an inhibitoryprinciple in liver plasma membranesarresting the growth of variousmammalian cells in vitro, Biochim. Biophys. Acta1982; 720:188�192.

  • P.A. Ascierto, S. Scala, G. Castello, A. Daponte, E.Simeone, A. Ottaiano, G. Beneduce, V.De Rosa, F. Izzo, M.T. Melucci, C.M. Ensor, A.W. Prestayko, F.W. Holtsberg, J.S. Bomalaski, M.A. Clark, N.Savaraj, L.G. Feun, T.F. Logan, Pegylated arginine deiminase treatment of patients with metastatic melanoma: results from phase I and II studies, J. Clin. Oncol. 2005; 23: 7660�7668.

  • RahamatUnissa, M. Sudhakar and A. Sunil Kumar Reddy. Screening of marine bacterial cultures for Extracellular production of l-arginine deiminases.World Journal of Pharmaceutical Research;2015: Vol 4, Issue 06.

  • RahamatUnissa, M. Sudhakar1 and A. Sunil Kumar Reddy. Condition Optimization and Production of Extracellular l-Arginine Deiminase f rom Vibr io alginolyt icus 1374.Cur rent Biotechnology;2015: 4, 254-260.

  • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-685.

  • Oginsky EL. Isolation and determination of arginine and citrulline. Meth Enzymol, 1957; 3: 639-643.

  • Lowry OH, Rosebrough NN, Farr AL, Randall RY.Proteinmeasurement with the folin phenol reagent.

  • J Biol Chem 1951;193:265-275.

  • Weickmann JL, Fahrney E. Arginine deiminase from Mycoplasma arthritidis. J Biol Chem 1977; 252:2615-2620.

  • Sugimura K, Fukuda S, Wada Y, et al.Identification and purification of arginine deiminase that originated from Mycoplasma sarginine. Infect Immun 1990; 58:2510-2515.

  • Mahdy NZ, Al-Tahan SS, Yaseen NY. Optimization of Arginine deiminase production from a local higher productive isolate Enterococcus faecium M1. Iraqi J Cancer Med Genet 2014; 1: 7-1.

  • Shibatani T, Kakimoto T, Chibata I. Crystallization and properties of L-arginine deiminase of Pseudomonas putida. J Biol Chem 1975; 250:4580-4583.

  • Wang Y, Li YZ. Cultivation to improve in vivo solubility of over expressed arginine deiminases in Escherichia coli and the enzyme characteristics. BMC Biotechnol 2014; 14:53.

  • Silvio Hering etal. Kinetic characterization of arginine deiminase and carbamate kinase from Streptococcus pyogenes M49. Protein Expression and Purification 2013;91 :61�68

  • T. Shibatani, T. Kakimoto, I. Chibata, Crystallization and properties of Larginine deiminase of Pseudomonas putida, J. Biol. Chem. 1975;250 : 4580�4583.

  • M.C. Manca de Nadra, A.A. Pesce de Ruiz Holgado, G. Oliver, Isolation and properties of arginine deiminase in Lactobacillus buchneri NCDO110, J. Appl. Biochem.1984; 6 :184�187.

  • T. Shibatani, T. Kakimoto and I. Chibata, J. Bioi. Chern.1975;250: 4580.

  • M.C. Manca de Nadra, A.A. Pesce de Ruiz Holgado, G. Oliver, Isolation and properties of arginine deiminase in Lactobacillus buchneri NCDO110, J. Appl. Biochem.1984; 6 : 184�187.

  • Cheng-Fu T et al. The Research of Enzymology Characterization about Arginine Deiminase from Enterococcus faecalis 2008; Microbiol, 35, 846-50.

  • Mining Co, Takaku H. A novel arginine deiminase, its manufacturing method and an anti-cancer agent containing this enzyme as an effective ingredient. Ltd./O Japan Energy Corporation. Patent 0414007, 1995.

  • Kim J et al. Arginine deiminase originating from Lactococcus lactis ssp. Lactis American Type Culture Collection (ATCC) 7962 induces G1-phase cell-cycle arrest and apoptosis in SNU-1 stomachadenocarcinoma cells Brit J Nutri 2009; 102: 1469�76.

  • Segal I. Biochemical Calculation. John Wiley and Sons: Inc. NewYork, 1976.

  • 01 January 2016

Year: 2016, Volume: 15, Issue: 1


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