Skip to main content
SpringerLink
Log in

Thermodynamic investigation of effect of salt concentrations on denatured α-Amylase adsorbed onto a moderately hydrophobic surface

  • Published:
Journal of Thermal Analysis and Calorimetry Aims and scope Submit manuscript

Abstract

The displacement adsorption enthalpies (ΔH) of denatured α-Amylase (by 1.8 mol L−1 GuHCl) adsorbed onto a moderately hydrophobic surface (PEG-600, the end-group of polyethylene glycol) from solutions (x mol L−1 (NH4)2SO4, 0.05 mol L−1 KH2PO4, pH 7.0) at 298 K are determined by microcalorimeter. Further, entropies (ΔS), Gibbs free energies (ΔG) and the fractions of ΔH, ΔS, and ΔG for net adsorption of protein and net desorption of water are calculated in combination with adsorption isotherms of α-Amylase based on the stoichiometric displacement theory for adsorption (SDT-A) and its thermodynamics. It is found that the displacement adsorptions of denatured α-Amylase onto PEG-600 surface are exothermic and enthalpy driven processes, and the processes of protein adsorption are accompanied with the hydration by which hydrogen bond form between the adsorbed protein molecules favor formation of β-sheet and β-turn structures. The Fourier transformation infrared spectroscopy (FTIR) analysis shows that the contents of ordered secondary structures of adsorbed α-Amylase increase with surface coverages and salt concentrations increment.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2

Similar content being viewed by others

References

  1. Kim KS, Kim S, Yang HJ, Kwon DY. Changes of glycinin conformation due to pH, heat and salt determined by DSC and CD. Int J Food Sci Technol. 2004;39:385–93.

    Article  CAS  Google Scholar 

  2. Lin FY, Chen CS, Chen WY. Yamamoto Sc. Microcalorimetric studies of the interaction mechanisms between proteins and Q-sepharose at pH near the isoelectric point (pI) effects of NaCl concentration, pH value, and temperature. J Chromatogr A. 2001;912:281–9.

    Article  CAS  Google Scholar 

  3. Bai SF, Dong AC. Effects of immobilization onto aluminum hydroxide particles on the thermally induced conformational behavior of three model proteins. Int J Biol Macromol. 2009;45:80–5.

    Article  CAS  Google Scholar 

  4. Geng XP, Wu YN, Wang BH, Zhang HF, Geng XD, Xing JW. Microcalorimetric determination of displacement adsorption enthalpies of protein refolding on a moderately hydrophobic surface at 308 K. J Therm Anal Calorim. 2006;85:601–8.

    Article  CAS  Google Scholar 

  5. Huang HM, Lin FY, Chen WY, Ruaan RC. Isothermal titration microcalorimetric studies of the effect of temperature on hydrophobic interaction between proteins and hydrophobic adsorbents. J Colloid Interface Sci. 2000;229:600–6.

    Article  CAS  Google Scholar 

  6. Bian LJ, Feng WK, Geng XD. Prediction of retention for protein in hydrophobic interaction chromatography. J Chromatogr (in chinese). 1991;9:267–70.

    CAS  Google Scholar 

  7. Tsai YS, Lin FY, Chen WY, Lin CC. Isothermal titration microcalorimetric studies of the effect of salt concentrations in the interaction between proteins and hydrophobic adsorbents. Colloids Surf A. 2002;197:111–8.

    Article  CAS  Google Scholar 

  8. Geng XP, Wu YN, Song JR, Geng XD, Xing JW, Lei ZM. Effect of salt concentrations on the displacement adsorption enthalpies of denatured protein folding at a moderately hydrophobic surface. J Therm Anal Calorim. 2006;85:593–600.

    Article  CAS  Google Scholar 

  9. Geng XP, Zheng MR, Wang BH, Lei ZM, Geng XD. Fractions of thermodynamic functions for native lysozyme adsorption onto moderately hydrophobic surface. J Therm Anal Calorim. 2008;93:503–8.

    Article  CAS  Google Scholar 

  10. Geng XP, Gao H, Wang BH, Liu AL, Feng XY. Thermodynamic analysis of denatured lysozyme folded on moderately hydrophobic surface at 298 K. J Therm Anal Calorim. 2009;95:345–52.

    Article  CAS  Google Scholar 

  11. Geng XD. Stoichiometric displacement theory and its application. Beijing: Science Press; 2004. (in chinese).

    Google Scholar 

  12. Geng XP, Han TS, Cao C. Adsorption enthalpy and desorption enthalpy during displacement of adsorbate to solvent in a liquid–solid system. J Therm Anal. 1995;45:157–65.

    Article  CAS  Google Scholar 

  13. Geng XP. Study on the fractions of thermodynamic function changes for both adsorption and desorption from a liquid–solid system. Thermochim Acta. 1998;308:131–8.

    Article  CAS  Google Scholar 

  14. Geng XP, Zhang HF, Wang BH, Geng XD, Xing JW. Calorimetric determination of enthalpies of lysozyme folding at a liquid–solid interface. J Therm Anal Calorim. 2005;82:193–9.

    Article  CAS  Google Scholar 

  15. Byler DM, Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers. 1986;25:469–87.

    Article  CAS  Google Scholar 

  16. Byler DM, Brouillette JN, Susi H. Quantitative studies of protein structure by FT-IR spectra deconvolution and curve-fitting. Spectroscopy. 1986;1:29–32.

    CAS  Google Scholar 

  17. Schwinté P, Voegel JC, Picart C, Haikel Y, Schaaf P, Szalontai B. Stabilizing effects of various polyelectrolyte multilayer films on the structure of adsorbed/embedded fibrinogen molecules: an ATR-FTIR study. J Phys Chem B. 2001;105:11906–16.

    Article  Google Scholar 

  18. Yan LF, Sun ZR. Protein molecule structure. Beijing: Tsinghua University Press; 1999. (in chinese).

    Google Scholar 

  19. Brandes N, Welzel PB, Werner C, Kroth LW. Adsorption-induced conformational changes of proteins onto ceramic particles: differential scanning calorimetry and FTIR analysis. J Colloid Interface Sci. 2006;299:56–9.

    Article  CAS  Google Scholar 

  20. Lu Y, Zhang WW, Wang GK. Progress in study of secondary structure of denaturized protein by FTIR. Spectrosc Spectr Anal (in chinese). 2008;28:88–93.

    Google Scholar 

  21. Lei ZM, Geng XP, Dai L, Geng XD. DSC and FTIR study of adsorbed lysozyme on hydrophobic surface. Spectrosc Spectr Anal (in chinese). 2008;28:2058–61.

    CAS  Google Scholar 

  22. Sane SU, Cramer SM, Przybycien TM. Protein structure perturbations on chromatographic surfaces. J Chromatogr A. 1999;849:149–59.

    Article  CAS  Google Scholar 

  23. Norde W, Favier JP. Structure of adsorbed and desorbed proteins. Colloids Surf. 1992;64:87–93.

    Article  CAS  Google Scholar 

Download references

Acknowledgements

We thank the National Natural Science Foundation of China for sponsoring the project (Grant No. 20673080).

Author information

Authors and Affiliations

  1. College of Environment & Chemical Engineering, Xi’an Polytechnic University, Xi’an, 710048, China

    X. Y. Feng, X. P. Geng, J. J. Peng & H. Y. Hou

  2. Institute of Modern Separation Science, Northwest University, Xi’an, 710069, China

    Q. Bai

Authors
  1. X. Y. Feng
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. X. P. Geng
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. J. J. Peng
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. H. Y. Hou
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Q. Bai
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to X. P. Geng.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Feng, X.Y., Geng, X.P., Peng, J.J. et al. Thermodynamic investigation of effect of salt concentrations on denatured α-Amylase adsorbed onto a moderately hydrophobic surface. J Therm Anal Calorim 102, 799–807 (2010). https://doi.org/10.1007/s10973-009-0611-5

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10973-009-0611-5

Keywords

Search

Navigation