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Evaluation of Chaperone-like Activity of Alginate: Microcapsule and Water-soluble Forms

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Abstract

To evaluate the chaperone-like activity of alginate stabilization and refolding of alkaline phosphatase (ALP) was investigated in the presence of alginate through two different approaches, the soluble form and microcapsule assisted methods. It was found that in the presence of microcapsules, ALP can be stabilized to a higher degree compared with the water-soluble form, whereas the denatured ALP is refolded with a higher yield through latter method. Lower refolding yields of alginate beads compared with its soluble form may be the result of lower refolding rate of ALP upon elution of the bound enzyme by dispersing the precipitate in NaCl which left the unfolded protein in an unsuitable environment, providing enough time for protein aggregation and leading finally to lower recovered activity compared with application of soluble form of alginate. In addition in the case of alginate capsules, the choice of suitable divalent ion is essential for stability and assistance in refolding.

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Abbreviations

ALP:

Alkaline phosphatase

BSA:

Bovine serum albumin

pNPP:

p-nitrophenyl phosphate

References

  1. Andi B, West AH, Cook P Arch (2004) Biochem Biophys 421:243–254

  2. Anisha GS, Prema P (2008) Bioresour Technol 99:3325–3330

    Google Scholar 

  3. Bradford MM (1976) Anal Biochem 72:248–254

    Article  CAS  Google Scholar 

  4. Cao Y, Shen X, Chen Y, Guo J, Chen Q, Jiang X (2005) Biomacromolecules 6:2189–2196

    Article  CAS  Google Scholar 

  5. Dong XY, Huang Y, Sun Y (2004) J Biochem 114:135–142

    CAS  Google Scholar 

  6. Dong XY, Shi JH, Sun Y (2002) Biotechnol Prog 18:11–19

    Article  Google Scholar 

  7. Fernández M, Fragoso A, Cao R, Baños M, Villalonga ML, Villalonga R (2002) Enzyme Microb Technol 24:1455–1459

    Google Scholar 

  8. Fernández M, Villalonga ML, Caballero J, Fragoso A, Cao R, Villalonga R (2003) Biotechnol Bioeng 83:743–747

    Google Scholar 

  9. Fosset M, Chappelet-Tordo D, Lazdunski M (1974) Biochemistry 13:1783–1788

    Article  CAS  Google Scholar 

  10. Garen A, Levinthal C (1960) Biophys Acta 38:470–483

    Article  CAS  Google Scholar 

  11. Gómez L, Villalonga R (2000) Biotechnol Lett 10:1191–1195

    Article  Google Scholar 

  12. Gombotz WR, Wee SF (1998) Adv Drug Deliv Rev 31:267–285

    Article  CAS  Google Scholar 

  13. Guex N, Peitsch MC (1997) Elecrophoresis 18:2714–2723

    Article  CAS  Google Scholar 

  14. Haug A (1961) Acta Chem Scand 15:1794–1799

    Article  CAS  Google Scholar 

  15. Haug A, Smidsrød O (1970) Acta Chem Scand 24:843–849

    Article  CAS  Google Scholar 

  16. Khodagholi F, Yazdanparast R (2007) Biochem Eng J 36:123–130

    Article  CAS  Google Scholar 

  17. Khodagholi F, Yazdanparast R (2008) Protein J 27:1–6

    Article  CAS  Google Scholar 

  18. Koepsell HJ, Tsuchiya HM (1952) J Bacteriol 63:293–295

    CAS  Google Scholar 

  19. Longo M, Combes D (1999) J Chem Technol Biotechnol 74:25–32

    Article  CAS  Google Scholar 

  20. Mateo C, Abian O, Fernandez-Lafuente R, Guisán Jv (2000) Enzyme Microb Technol 26:509–515

    Google Scholar 

  21. Minagawa H, Kaneko H (2000) Biotechnol Lett 22:1131–1133

    Google Scholar 

  22. Mørch YA, Donati I, Strand BL, Skjåk-Braek G (2006) Biomacromolecules 7:1471–1480

    Article  Google Scholar 

  23. Rastello De Boisseson M, Leonard M, Hubert P, Marchal P, Stequert A, Castel C, Favre E, Dellacherie E (2004) J Colloid Interface Sci 273:131–139

    Article  CAS  Google Scholar 

  24. Ren B, Gao Y, Lu L, Liu X, Tong Z (2006) Carbohydr Polym 66:266–273

    Article  CAS  Google Scholar 

  25. Reyes N, Rivas-Ruiz I, Domínguez-Espinosa R, Solís S (2006) Biochem Eng J 32:43–48

    Google Scholar 

  26. Roy I, Jain S, Teotia S, Gupta MN (2004) Biotechnol Prog 20:1490–1495

    Article  CAS  Google Scholar 

  27. Saboury AA, Karbassi F, Haghbeen K, Ranjbar B, Moosavi-Movahedi AA, Farzami B (2004) Int J Biol Macromol 34:257–262

    Google Scholar 

  28. Sattarahmady N, Khodagholi F, Moosavi-Movahedi AA, Heli H, Hakimelahi GH (2007) Int J Biol Macromol 41:180–184

    Article  CAS  Google Scholar 

  29. Shamala TR, Prasad MS (1995) Biochemistry 30:237–241

    Google Scholar 

  30. Silva CM, Ribeiro AJ, Figueiredo IV, Gonçalves AR, Veiga F (2006) Int J Pharm 311:1–10

    Article  CAS  Google Scholar 

  31. Siva Sai Kumar R, Vishwanath KS, Singh SA, Appu Rao AG (2006) Process Biochem 41:2282–2288

    Google Scholar 

  32. Sriamornsak P, Sungthongjeen S (2007) AAPS Pharm Sci Tech 8:3 (article 51)

    Google Scholar 

  33. Tayyab S, Ahmad B, Kumar Y, Khan MM (2002) Int J Biol Macromol 30:17–22

    Article  CAS  Google Scholar 

  34. Thu B, Bruheim P, Espevik T, Smidsrød O, Soon-Shiong P, Skjåk-Braek G (1996) Biomaterials 17:1069–1079

    Article  CAS  Google Scholar 

  35. Villalonga R, Fernández M, Fragoso A, Cao R, Di Pierro P, Mariniello L, Porta R (2003) Biotechnol Bioeng 81:732–737

    Article  CAS  Google Scholar 

  36. Villalonga R, Villalonga ML, Gómez L (2000) Mol J Catal B Enzym 10:483–490

    Article  CAS  Google Scholar 

  37. Wang J, Lu D, Lin Y, Liu Zh (2005) Biochem Chem 24:269–277

    CAS  Google Scholar 

  38. Wang W (2005) Int J Pharm 289:1–30

    Article  CAS  Google Scholar 

  39. Zhang YX, Zhu Y, Xi HW, Liu YL, Zhou HM (2002) Int J Biochem Cell Biol 34:1241–1247

    Article  CAS  Google Scholar 

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Acknowledgments

We would like to thank the research council of the Shahid Beheshti University (M. C.) for the financial support of this investigation.f

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Authors and Affiliations

  1. Neuroscience Research Center, Shahid Beheshti University (M. C.), Tehran, Iran

    Neguine Rezaii & Fariba Khodagholi

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  1. Neguine Rezaii
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  2. Fariba Khodagholi
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Correspondence to Fariba Khodagholi.

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Rezaii, N., Khodagholi, F. Evaluation of Chaperone-like Activity of Alginate: Microcapsule and Water-soluble Forms. Protein J 28, 124–130 (2009). https://doi.org/10.1007/s10930-009-9172-5

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