Investigation of Effective Factors on the Optimization of Surface Layer Protein Production in the Deinococcus radiodurans R1 Strain using Response Surface Method

Ebadi Sharaf abad, Behruz; Khalilzadeh, Rassoul; Alijanianzadeh, Mahdi; Abdolirad, Maryam

year 11, Issue 3 (July - August 2017) Iran J Med Microbiol 2017, 11(3): 59-70 | Back to browse issues page

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Ebadi Sharaf abad B, Khalilzadeh R, Alijanianzadeh M, Abdolirad M. Investigation of Effective Factors on the Optimization of Surface Layer Protein Production in the Deinococcus radiodurans R1 Strain using Response Surface Method . Iran J Med Microbiol 2017; 11 (3) :59-70
URL: http://ijmm.ir/article-1-680-en.html

Investigation of Effective Factors on the Optimization of Surface Layer Protein Production in the Deinococcus radiodurans R1 Strain using Response Surface Method

Behruz Ebadi Sharaf abad¹

, Rassoul Khalilzadeh

², Mahdi Alijanianzadeh¹

, Maryam Abdolirad¹

1- Department of Bioscience and Biotechnology, Malek Ashtar University of Technology, Tehran, Iran
2- Department of Bioscience and Biotechnology, Malek Ashtar University of Technology, Tehran, Iran , rkhalilzadeh@mut.ac.ir

Abstract: (8259 Views)

Background and Aims: Due to its self-assembly properties on variety of surfaces and creating regular functional groups, surface layer protein isolated from bacteria, has significant applications in the field of nanobiotechnology such as biosensor production, targeting drug delivery systems and tissue engineering. In this research, optimization of discontinuous culture medium compositions for the production of HPI surface layer protein from Deinococcus radiodurans R₁ strain was performed using the response surface (RSM) method.
Materials and Methods: In 2016, culture medium for 16 designed experiments with fractional factorial analysis (FFA) was prepared and effective factors among six variables of the discontinuous culture medium was investigated for the production of surface layer proteins of D.radiodurans R₁. Twenty experiments were then designed for the optimization of effective variables using central composite design (CCD) method. Surface protein purity was assessed using SDS-PAGE analysis and its concentration was calculated via Bradford method.
Results: The optimized medium containing 13.36 g/L glucose, 5 g/L yeast extraction, 5 g/L tryptone, 2 g/L HEPES buffer, 0.55 MgSO₄*7H₂O, 0.0368 g/L MnCl₂*4 H₂O, was determined. Wet cellular mass was found as 16.87 g/L, which is 24% more than TGY basic medium and 74% much more than TYG culture medium including NaCl.
Conclusions: Results of the Bradford method demonstrated that the concentration of surface layer protein HPI isolated from D. radiodurans R₁ was 5.6 mg which was more than twice of that using 1liter of basic TGY medium.

Keywords: Deinococcus radiodurans R1, S-layer protein, Response surface methodology (RSM)

Full-Text [PDF 1119 kb] (2689 Downloads)

Type of Study: Original Research Article | Subject: Nanotechnology In Medicine
Received: 2017/03/2 | Accepted: 2017/06/14 | ePublished: 2017/08/8

References

1. Vincent JF, Bogatyreva OA, Bogatyrev NR, Bowyer A, Pahl AK. Biomimetics: its practice and theory. J R Soc. Interface 2006; 3(9):471-82.

2. Xiao S, Liu F, Rosen AE, Hainfeld JF, Seeman NC, Musier-Forsyth K, et al. Selfassembly of metallic nanoparticle arrays by DNA scaffolding. J Nanopart Res 2002; 4(4):313-7.

3. Toca‐Herrera JL, Krastev R, Bosio V, Küpcü S, Pum D, Fery A, et al. Recrystallization of Bacterial S‐Layers on Flat Polyelectrolyte Surfaces and Hollow Polyelectrolyte Capsules. Small 2005; 1(3):339-48.

4. Pastorino L, Soumetz FC, Giacomini M, Ruggiero C. Development of a piezoelectric immunosensor for the measurement of paclitaxel. J Immunol Methods 2006; 313(1):191-8.

5. Habibi N, Pastorino L, Soumetz FC, Sbrana F, Raiteri R, Ruggiero C. Nanoengineered polymeric S-layers based capsules with targeting activity. Colloids Surf., B 2011; 88(1):366-72.

6. Tschiggerl H, Casey JL, Parisi K, Foley M, Sleytr UB. Display of a peptide mimotope on a crystalline bacterial cell surface layer (S-layer) lattice for diagnosis of Epstein–Barr virus infection. Bioconjugate Chem 2008; 19(4):860-5.

7. Weigert S, Sára M. Surface modification of an ultrafiltration membrane with crystalline structure and studies on interactions with selected protein molecules. J Membr Sci 1995; 106(1-2):147-59.

8. Habibi N, Zohrabi T. Isolation of S-Layer from Caulobacter and re-crystallization on planar supports. Biological Journal Of Microorganism 2015; 4(13).

9. Sleytr UB, Bayley H, Sára M, Breitwieser A, Küpcü S, Mader C. Applications of S-layers. FEMS Microbiol Rev 1997; 20(1-2):151-75.

10. Debabov VG. Bacterial and archaeal S-layers as a subject of nanobiotechnology. Mol Biol 2004; 38(4):482-93.

11. Nakamura H, Karube I. Current research activity in biosensors. Anal Bioanal Chem 2003; 377(3):446-68.

12. Lu B, Smyth MR, O'Kennedy R. Tutorial review. Oriented immobilization of antibodies and its applications in immunoassays and immunosensors. Analyst1996; 121(3):29R-32R.

13. Abdolirad M, Khalilzadeh R, Alijanianzadeh M. Isolation and Study of S-layer Nanostructure of Deinococcus Radiodurans R1. Biomacromolecular Journal, 2016; 2(2): 126-134

14. Rothfuss H, Lara JC, Schmid AK, Lidstrom ME. Involvement of the S-layer proteins Hpi and SlpA in the maintenance of cell envelope integrity in Deinococcus radiodurans R1. Microbiology 2006; 152(9):2779-87.

15. Farci D, Bowler MW, Esposito F, McSweeney S, Tramontano E, Piano D. Purification and characterization of DR_2577 (SlpA) a major S-layer protein from Deinococcus radiodurans. Front Microbiol 2015; 6:414.

16. Hall SR, Shenton W, Engelhardt H, Mann S. Site‐Specific Organization of Gold Nanoparticles by Biomolecular Templating. Chem Phys Chem 2001; 2(3):184-6.

17. Bergkvist M, Mark SS, Yang X, Angert ER, Batt CA. Bionanofabrication of ordered nanoparticle arrays: effect of particle properties and adsorption conditions. J Phys Chem B 2004; 108(24):8241-8.

18. Allred DB, Sarikaya M, Baneyx F, Schwartz DT. Electrochemical nanofabrication using crystalline protein masks. Nano Lett. 2005; 5(4):609-13.

19. Mark SS, Bergkvist M, Yang X, Teixeira LM, Bhatnagar P, Angert ER and et al. Bionanofabrication of metallic and semiconductor nanoparticle arrays using S-layer protein lattices with different lateral spacing and geometries. Langmuir 2006; 22(8):3763-74.

20. Sierra-Sastre Y, Dayeh SA, Picraux ST, Batt CA. Epitaxy of Ge nanowires grown from biotemplated Au nanoparticle catalysts. ACS nano 2010; 4(2):1209-17.

21. Nosonovsky M, Bhushan B. Wetting of rough three-dimensional superhydrophobic surfaces. Microsys Technol 2006; 12(3):273-81.

22. Ohring M. Materials science of thin films. Academic press; 2001 Oct 20.

23. Peteu SF, Szunerits S, Vasilescu A, Knoll W. Nanoscale Architectures for Smart Bio-Interfaces: Advances and Challenges. Nanofabrication Intech, Yoshitake Masuda (Ed.) 2011. P. 63-98.

24. Holland AD, Rothfuss HM, Lidstrom ME. Development of a defined medium supporting rapid growth for Deinococcus radiodurans and analysis of metabolic capacities. Appl Microbiol Biotechnol 2006; 72(5):1074-82.

25. He Y. High cell density production of Deinococcus radiodurans under optimized conditions. J Ind Microbiol Biotechnol 2009; 36(4):539-46.

26. Li C, Bai J, Cai Z, Ouyang F. Optimization of a cultural medium for bacteriocin production by Lactococcus lactis using response surface methodology. J Biotechnol. 2002; 93(1):27-34.

27. Box GE, Wilson KB. On the experimental attainment of optimum conditions. In Break throughs in Statistics. Springer New York; 1992, p. 270-310.

28. Farci D, Bowler MW, Esposito F, McSweeney S, Tramontano E, Piano D. Purification and characterization of DR_2577 (SlpA) a major S-layer protein from Deinococcus radiodurans. Front Microbiol. 2015; 6:414.

29. Zeinoddini M.Theoretical and practical guide to protein analysis methods. 1st.Tehran: Malek Ashtar University of Technology Press. 2011. [in Persian]

30. Misra CS, Basu B, Apte SK. Surface (S)-layer proteins of Deinococcus radiodurans and their utility as vehicles for surface localization of functional proteins. Biochim Biophys Acta 2015; 1848(12):3181-7.