The Protein Journal

, Volume 26, Issue 5, pp 293–301

Comparative Evaluation of α-Amylase Refolding Through Two Different Artificial Chaperone Systems

  • Fariba Khodagholi
  • Bahareh Eftekharzadeh
  • Razieh Yazdanparast
Article

DOI: 10.1007/s10930-007-9071-6

Cite this article as:
Khodagholi, F., Eftekharzadeh, B. & Yazdanparast, R. Protein J (2007) 26: 293. doi:10.1007/s10930-007-9071-6
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Abstract

Two different artificial chaperone systems were evaluated in this work using either detergents or CDs as the stripping agents. Upon dilution of urea-denatured α-amylase to a non-denaturing urea concentration in the presence of the capturing agent, complexes of the detergent and non-native protein molecules are formed and thereby the formation of protein aggregates is prevented. The so-called captured protein is unable to refold from the detergent-protein complex states unless a stripping agent is used to remove the detergent molecules. Our results by fluorescence, UV, turbidity measurement, circular dichroism, surface tension and activity assay indicated that the extent of refolding assistance was different due to different inter- and intra- molecular interactions in the two different systems. However, the high activity recovery in the presence of detergents, as the stripping agent, suggests that they can constitute suitable replacement for the more expensive and common stripping agent of cyclodextrins.

Keywords

α-Amylaseanionic detergentsartificial chaperoneBacillus subtiliscationic detergentscyclodextrinsrefolding

Copyright information

© Springer Science+Business Media, LLC 2007

Authors and Affiliations

  • Fariba Khodagholi
    • 1
  • Bahareh Eftekharzadeh
    • 2
  • Razieh Yazdanparast
    • 1
  1. 1.Institute of Biochemistry and BiophysicsThe University of TehranTehranIran
  2. 2.Department of Medicinal chemistry, Faculty of PharmacyTehran University of Medical ScienceTehranIran