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  • 1 Xi'an University of Engineering Science & Technology, College of Environment & Chemical Engineering Xi'an 710048, China, Xi'an 710048, China,
  • | 2 Xi'an University of Engineering Science & Technology, College of Environment & Chemical Engineering Xi'an 710048, China Xi'an 710048, China
  • | 3 Institute of Physical Chemistry, Peaking University Beijing 100871, China Beijing 100871, China
  • | 4 Institute of Modern Separation Science, Northwest University Xi'an 710069, China Xi'an 710069, China
  • | 5 Xi'an University of Engineering Science & Technology, College of Textile Engineering & Material Xi'an 710048, China Xi'an 710048, China
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Summary  

Calorimetric determination of the total enthalpy changes (ΔHi) of guanidine-denatured lysozyme (Lys) during the adsorption with simultaneously refolding on the surface of hydrophobic interaction chromatography packings was carried out at 250.001C. The measured ΔHiin the circumstances should include the changes in the three fractions: adsorption, dehydration and molecular conformation. It was found that when the unfolded Lys molecules are adsorbed and refold on the surface, entropy-driving caused by the dehydration of Lys mainly dominates the foregoing process. The refolding enthalpies of Lys, ΔΔHiwere found to be 10~100 folds higher than that measured in usual solutions.</o:p>

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