Advertisement

Research on Chemical Intermediates

, Volume 45, Issue 4, pp 2489–2501 | Cite as

A fast and efficient stabilization of firefly luciferase on MIL-53(Al) via surface adsorption mechanism

  • Zohreh Nowroozi-Nejad
  • Bahram BahramianEmail author
  • Saman Hosseinkhani
Article
  • 16 Downloads

Abstract

Stabilization and immobilization on a proper support is essential in processing and production of enzymes. Luciferase is an unstable, thermally sensitive, and light-emitting enzyme that requires stabilization for efficiency and productivity in bio-luminescence reactions. In this work, a known and well-porous framework, MIL-53(Al), was used, for the first time, to support the immobilization of firefly luciferase. Interestingly, all the stability values were improved through the immobilization process, and the content of the loading enzyme on MIL-53(Al) was found to be significant. The results obtained indicated that the stabilization of firefly luciferase on MIL-53(Al) proceeded through the adsorption method. MIL-53(Al) was also characterized by the FT-IR, X-ray diffraction, FE-SEM, TEM, BET, and TGA techniques in order to determine the carboxylic groups and symmetric/asymmetric CO2, percentage of crystallinity and its purity, morphology, size, and shape of the MIL-53(Al) particles, and surface-to-area ratio and thermal gravimetry of support.

Graphical abstract

Keywords

Immobilization of luciferase MIL-53(Al) Surface adsorption Enzyme immobilization Metal organic frameworks 

Notes

Acknowledgements

The authors appreciate the support of Shahrood University of Technology and the Research Council of Tarbiat Modares University of Biological Sciences for the financial support of this work.

References

  1. 1.
    L. Marron-Brignone, R. Morélis, L. Blum, P. Coulet, Thin Solid Films 284, 784 (1996)CrossRefGoogle Scholar
  2. 2.
    N. Ugarova, L.Y. Brovko, E. Beliaieva, Enzyme Microb. Technol. 5, 60 (1983)CrossRefGoogle Scholar
  3. 3.
    A.R. Ribeiro, R.M. Santos, L.M. Rosário, M.H. Gil, J. Biolumin. Chemilumin. 13, 371 (1998)CrossRefGoogle Scholar
  4. 4.
    Y. Lee, I. Jablonski, M. DeLuca, Anal. Biochem. 80, 496 (1977)CrossRefGoogle Scholar
  5. 5.
    C.H. Ho, L. Limberis, K.D. Caldwell, R.J. Stewart, Langmuir 14, 3889 (1998)CrossRefGoogle Scholar
  6. 6.
    W. Wang, Q. Zhao, M. Luo, M. Li, D. Wang, Y. Wang, Q. Liu, A.C.S. Appl, Mater. Interfaces 7, 20046 (2015)CrossRefGoogle Scholar
  7. 7.
    M.H. Pham, G.T. Vuong, A.T. Vu, T.O. Do, Langmuir 27, 15261 (2011)CrossRefGoogle Scholar
  8. 8.
    Y.L. Liu, X.J. Zhao, X.X. Yang, Y.F. Li, Analyst 138, 4526 (2013)CrossRefGoogle Scholar
  9. 9.
    B. Chen, S. Xiang, G. Qian, ACC. Chem. Res. 43, 1115 (2010)CrossRefGoogle Scholar
  10. 10.
    X. Zhu, H. Zheng, X. Wei, Z. Lin, L. Guo, B. Qiu, G. Chen, Chem. Commun. 49, 1276 (2013)CrossRefGoogle Scholar
  11. 11.
    F.A. Erhardt, H.J. Jordening, J. Biotechnol. 131, 440 (2007)CrossRefGoogle Scholar
  12. 12.
    E. Magner, Chem. Soc. Rev. 42, 6213 (2013)CrossRefGoogle Scholar
  13. 13.
    C. Thorn, H. Gustafsson, L. Olsson, J. Mol. Catal. B Enzym. 72, 57 (2011)CrossRefGoogle Scholar
  14. 14.
    A. Salis, M.F. Casula, M.S. Bhattacharyya, M. Pinna, V. Solinas, M. Monduzzi, Chem. Cat. Chem. 2, 322 (2010)Google Scholar
  15. 15.
    Q. Liu, X. Kong, C. Zhang, Y. Chen, Y. Hua, J. Sci. Food Agric. 93, 1953 (2013)CrossRefGoogle Scholar
  16. 16.
    Y. Zhang, Q. Gao, Z. Lin, T. Zhang, J. Xu, Y. Tan, W. Tian, Sci. Rep. 4, 4947 (2014)CrossRefGoogle Scholar
  17. 17.
    X. Wu, M. Hou, J. Ge, Catal. Sci. Technol. 5, 5077 (2015)CrossRefGoogle Scholar
  18. 18.
    T.J. Pisklak, M. Macías, D.H. Coutinho, R.S. Huang, K.J. Balkus, Top. Catal. 38, 269 (2006)CrossRefGoogle Scholar
  19. 19.
    V. Lykourinou, Y. Chen, X.S. Wang, L. Meng, T. Hoang, L.J. Ming, R.L. Musselman, S. Ma, J. Am. Chem. Soc. 133, 10382 (2011)CrossRefGoogle Scholar
  20. 20.
    W. Ma, Q. Jiang, P. Yu, L. Yang, L. Mao, Anal. Chem. 85, 7550 (2013)CrossRefGoogle Scholar
  21. 21.
    W.L. Liu, N.S. Yang, Y.T. Chen, S. Lirio, C.Y. Wu, C.H. Lin, H.Y. Huang, Chem. Eur. J. 21, 115 (2015)CrossRefGoogle Scholar
  22. 22.
    S. Patra, S. Sene, C. Mousty, C. Serre, A. Chaussé, L. Legrand, N. Steunou, A.C.S. Appl, Mater. Interfaces 8, 20012 (2016)CrossRefGoogle Scholar
  23. 23.
    V. Gascón, E. Castro-Miguel, M. Díaz-García, R.M. Blanco, M. Sanchez-Sanchez, J. Chem. Technol. Biotechnol. 92, 2583 (2017)CrossRefGoogle Scholar
  24. 24.
    X. Qian, Z. Zhong, B. Yadian, J. Wu, K. Zhou, J.S.K. Teo, L. Chen, Y. Long, Y. Huang, Int. J. Hydrog. Energy 39, 14496 (2014)CrossRefGoogle Scholar
  25. 25.
    M.M. Bradford, Anal. Biochem. 72, 248 (1976)CrossRefGoogle Scholar
  26. 26.
    W.P. Mounfield III, K.S. Walton, J. Colloid Interface Sci. 447, 33 (2015)CrossRefGoogle Scholar
  27. 27.
    C. Tudisco, G. Zolubas, B. Seoane, H.R. Zafarani, M. Kazemzad, J. Gascon, P.L. Hagedoorn, L. Rassaei, RSC Adv. 6, 108051 (2016)CrossRefGoogle Scholar
  28. 28.
    M. Wang, X. Zhang, L.Z. Hou, Y. Chen, Aerosol Air Qual. Res. 16, 2003 (2016)CrossRefGoogle Scholar
  29. 29.
    E. Rahmani, M. Rahmani, Ind. Eng. Chem. Res. 57, 169 (2017)CrossRefGoogle Scholar
  30. 30.
    T. Loiseau, C. Serre, C. Huguenard, G. Fink, F. Taulelle, M. Henry, T. Bataille, G. Fÿrey, Chem. Eur. J. 10, 1373 (2004)CrossRefGoogle Scholar
  31. 31.
    L.A. Tai, Y.T. Kang, Y.C. Chen, Y.C. Wang, Y.J. Wang, Y.T. Wu, K.L. Liu, C.Y. Wang, Y.F. Ko, C.Y. Chen, N.C. Huang, J.K. Chen, Y.F. Hsieh, T.R. Yew, C.S. Yang, Anal. Chem. 84, 6312 (2012)CrossRefGoogle Scholar
  32. 32.
    N.R. Mohamad, N.H.C. Marzuki, N.A. Buang, F. Huyop, R.A. Wahab, Biotechnol. Biotechnol. Equip. 29, 205 (2015)CrossRefGoogle Scholar
  33. 33.
    J.G. Nguyen, S.M. Cohen, J. Am. Chem. Soc. 132, 4560 (2010)CrossRefGoogle Scholar
  34. 34.
    X. Lian, Y. Fang, E. Joseph, Q. Wang, J. Li, S. Banerjee, C. Lollar, X. Wang, H.C. Zhou, Chem. Soc. Rev. 46, 3386 (2017)CrossRefGoogle Scholar
  35. 35.
    M. Alhamami, H. Doan, C.H. Cheng, Materials 7, 3198 (2014)CrossRefGoogle Scholar
  36. 36.
    M.G. Roig, F.B. Estevez, F.G. Velasco, J.M. Cachaza, Biochem. Educ. 15, 33 (1987)CrossRefGoogle Scholar
  37. 37.
    L. Goldstcin, Y. Lcvin, E. Katchalski, Biochemistry 3, 1913 (1964)CrossRefGoogle Scholar
  38. 38.
    E.K. Pye, B. Chance, Methods, in Enzymology, ed. by K. Moshach (Academic Press, New York, 1976), p. 357Google Scholar
  39. 39.
    A. Bar-Eli, E. Katchalski, J. Biol. Chem. 238, 1690 (1963)Google Scholar
  40. 40.
    K.J. Laidler, P.S. Bunting, Methods, in Enzymology, ed. by D.L. Purich (Academic Press, New York, 1980), p. 227Google Scholar

Copyright information

© Springer Nature B.V. 2019

Authors and Affiliations

  1. 1.Faculty of Chemistry, Shahrood University of TechnologyShahroodIran
  2. 2.Department of BiochemistryFaculty of Biological Sciences, Tarbiat Modares UniversityTehranIran

Personalised recommendations