Isolation, Purification and Antimicrobial Efficacy of Ovotransferrin from Eggs of Broiler, Domestic and Quail

Authors

  • Sampath Kumar G  Asst. Professor, Department of Biochemistry, Vel's Institute of Science, Technology & Advanced Studies, Pallavaram, Chennai, Tamil Nadu, India
  • Anitha  Department of Biochemistry, Vel's Institute of Science, Technology & Advanced Studies, Pallavaram, Chennai, Tamil Nadu, India
  • Preethi L  Department of Genetics, Dr ALMPGIBMS, University of Madras, Taramani, Chennai – 600113
  • Arunkumar R  Scientist, Department of Medical Research Unit, MMC, Chennai, Tamil Nadu, India
  • Ilakkiya A  Asst. Professor, Department of Biochemistry, Vel's Institute of Science, Technology & Advanced Studies, Pallavaram, Chennai, Tamil Nadu, India
  • Selvakumar K  Head- Department of Clinical Biochemistry, Billroth Hospitals, Shenoy Nagar, Chennai Tamil Nadu, India

DOI:

https://doi.org//10.32628/IJSRST207385

Keywords:

Otrf,AMPC,SDS-PAGE

Abstract

Ovotransferrin is one of the major egg white proteins that have antimicrobial activity as well as iron binding capability. The objective of this study was to develop a simple and easy method to separate ovotransferrin using organic solvents. The purity of the ovotransferrin was determined using SDS-PAGE, the isolated protein was further studied for the assessment of interaction between food borne pathogens and the isolated Otrf by protein-protein molecular docking. However, this method is simpler and more cost effective than the previous method. The isolated ovotransferrin can be used as is or after modifications for various applications such as antimicrobial treatments. Recently, the iron chelating activity of Otrf has been exposed to upsurge the stimulus by an inhibitor of AMPc

References

  1. Abeyrathne ED, Lee HY, Ahn DU. Egg white proteins and their potential use in food processing or as nutraceutical and pharmaceutical agents—A review. Poultry Science. 2013;92:3292-9.
  2. Wei Z, Huang Q. Modification of ovotransferrin by Maillard reaction: Consequences for structure, fibrillation and emulsifying property of fibrils. Food Hydrocolloids. 2019;97:105186.
  3. Ko KY, Ahn DU. An economic and simple purification procedure for the large-scale production of ovotransferrin from egg white. Poultry science. 2008;87:1441-50.
  4. Giansanti F, Leboffe L, Pitari G, Ippoliti R, Antonini G. Physiological roles of ovotransferrin. Biochimica et Biophysica Acta (BBA)-General Subjects. 2012;1820:218-25.
  5. Baron F, Jan S. Egg and egg product microbiology. InImproving the safety and quality of eggs and egg products. Woodhead Publishing. 2011;330-350.
  6. Baron F, Jan S, Gonnet F, Pasco M, Jardin J, Giudici B, Gautier M, Guérin-Dubiard C, Nau F. Ovotransferrin plays a major role in the strong bactericidal effect of egg white against the Bacillus cereus group. Journal of food protection. 2014;77:955-62.
  7. Ibrahim HR, Sugimoto Y, Aoki T. Ovotransferrin antimicrobial peptide (OTAP-92) kills bacteria through a membrane damage mechanism. Biochimica et Biophysica Acta (BBA)-General Subjects. 2000 ;1523:196-205.
  8. Gupta RC, Srivastava A, Lall R, editors. Nutraceuticals in Veterinary Medicine. Springer; 2019.
  9. Alabdeh M, Lechevalier V, Nau F, Gautier M, Cochet MF, Gonnet F, Jan S, Baron F. Role of incubation conditions and protein fraction on the antimicrobial activity of egg white against Salmonella Enteritidis and Escherichia coli. Journal of food protection. 2011;74::24.
  10. Park RY, Choi MH, Sun HY, Shin SH. Production of catechol-siderophore and utilization of transferrin-bound iron in Bacillus cereus. Biological and Pharmaceutical Bulletin. 2005;28:1132-5.
  11. Page MG. Siderophore conjugates. Annals of the New York Academy of Sciences. 2013;1277:115-26.
  12. Babini GS, Livermore DM. Effect of conalbumin on the activity of Syn 2190, a 1, 5 dihydroxy-4-pyridon monobactam inhibitor of AmpC β-lactamases. Journal of Antimicrobial Chemotherapy. 2000;45:105-9.
  13. Nukaga M, Kumar S, Nukaga K, Pratt RF, Knox JR. Hydrolysis of third-generation cephalosporins by class C β-lactamases structures of a transition state analog of cefotaxime in wild-type and extended spectrum enzymes. Journal of Biological Chemistry. 2004;279:9344.
  14. Jacobs MR, Abdelhamed AM, Good CE, Rhoads DD, Hujer KM, Hujer AM, Domitrovic TN, Rudin SD, Richter SS, van Duin D, Kreiswirth BN. ARGONAUT-I: activity of cefiderocol (S-649266), a siderophore cephalosporin, against gram-negative bacteria, including carbapenem-resistant nonfermenters and Enterobacteriaceae with defined extended-spectrum β-lactamases and carbapenemases. Antimicrobial agents and chemotherapy. 2019;63:e01801-18.
  15. Gould IM, Bal AM. New antibiotic agents in the pipeline and how they can help overcome microbial resistance. Virulence. 2013;4:185-91.
  16. Basmaci R, Bielicki J, Daniels R, Kissoon N, Ellis S, Balasegaram M, Sharland M. Management of children with multidrug-resistant sepsis in low-income and middle-income countries. The Lancet Child & Adolescent Health. 2018;2:8-10.
  17. Ito A, Sato T, Ota M, Takemura M, Nishikawa T, Toba S, Kohira N, Miyagawa S, Ishibashi N, Matsumoto S, Nakamura R. In vitro antibacterial properties of cefiderocol, a novel siderophore cephalosporin, against Gram-negative bacteria. Antimicrobial agents and chemotherapy. 2018;62:e01454-17.
  18. Ruppé É, Woerther PL, Barbier F. Mechanisms of antimicrobial resistance in Gram-negative bacilli. Annals of intensive care. 2015;5:21.
  19. McPherson CJ, Aschenbrenner LM, Lacey BM, Fahnoe KC, Lemmon MM, Finegan SM, Tadakamalla B, O'Donnell JP, Mueller JP, Tomaras AP. Clinically relevant Gram-negative resistance mechanisms have no effect on the efficacy of MC-1, a novel siderophore-conjugated monocarbam. Antimicrobial agents and chemotherapy. 2012;56:6334-42.
  20. McNamara DJ. The fifty year rehabilitation of the egg. Nutrients. 2015;7:8716-22.
  21. Giansanti F, Leboffe L, Pitari G, Ippoliti R, Antonini G. Physiological roles of ovotransferrin. Biochimica et Biophysica Acta (BBA)-General Subjects. 2012;1820:218-25.
  22. Price NC, Nairn J. Exploring proteins: a student's guide to experimental skills and methods. Oxford, UK: Oxford University Press; 2009.
  23. Hopkins FG. On the separation of a pure albumin from egg-white. The Journal of physiology. 1900 ;25:306.
  24. Chick H, Martin CJ. The precipitation of egg-albumin by ammonium sulphate. A contribution to the theory of the “salting-out” of proteins. Biochemical Journal. 1913;7:380.
  25. H Wu J. Eggs and egg products processing. Food processing: Principles and applications. 2014 Apr 7:437-55.u S, Qiu N, Liu Y, Zhao H, Gao D, Song R, Ma M. Identification and comparative proteomic study of quail and duck egg white protein using 2-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry analysis. Poultry science. 2016 ;95:1137-44

International Journal of Scientific Research in Science and Technology

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Published

2020-06-30

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Volume 7, Issue 3, May-June-2020

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Research Articles

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How to Cite

[1]
Sampath Kumar G, Anitha, Preethi L, Arunkumar R, Ilakkiya A, Selvakumar K, " Isolation, Purification and Antimicrobial Efficacy of Ovotransferrin from Eggs of Broiler, Domestic and Quail , International Journal of Scientific Research in Science and Technology(IJSRST), Online ISSN : 2395-602X, Print ISSN : 2395-6011, Volume 7, Issue 3, pp.405-414, May-June-2020. Available at doi : https://doi.org/10.32628/IJSRST207385