Journal of Thermal Analysis and Calorimetry
Volume/Issue:
Volume 85: Issue 3
Microcalorimetric determination of displacement adsorption enthalpies of protein refolding on a moderately hydrophobic surface at 308 K
Authors:
X. Geng Xi’an Politechnic University College of Environment and Chemical Engineering Xi’an China 710048 Xi’an China 710048

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Y. Wu Xi’an Politechnic University College of Environment and Chemical Engineering Xi’an China 710048 Xi’an China 710048

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B. Wang Peaking University Institute of Physical Chemistry Beijing China 100871 Beijing China 100871

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H. Zhang Xi’an Politechnic University College of Environment and Chemical Engineering Xi’an China 710048 Xi’an China 710048

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X. Geng Northwest University Institute of Modern Separation Science Xi’an China 710069 Xi’an China 710069

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J. Xing Xi’an Politechnic University College of Textile Engineering and Material Xi’an China 710048 Xi’an China 710048

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Pages:
601–608
Online Publication Date:
15 Sep 2006
Publication Date:
01 Sep 2006
Article Category:
Research Article
DOI:
https://doi.org/10.1007/s10973-006-7645-8
Keywords:
displacement adsorption enthalpy; hydrophobic interaction mechanism; liquid/solid system; lysozyme; microcalorimetry; protein folding
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Abstract  

Both microcalorimetric determination of displacement adsorption enthalpies ΔH and measurement of adsorbed amounts of guanidine – denatured lysozyme (Lys) refolding on the surface of hydrophobic interaction chromatography (HIC) packings at 308 K were carried out and compared with that at 298 K. Study shows that both temperature and concentration of guanidine hydrochloride (GuHCl) affect the molecular mechanism of hydrophobic interaction of protein with adsorbent based on the analysis of dividing ΔH values into three kinds of enthalpy fractions. The adsorption in higher concentrations of GuHCl (>1.3 mol L–1) at 308 K is an enthalpy-driving process, and the adsorption under other GuHCl concentrations is an entropy-driving process. The fact that the Lys denatured by 1.8 mol L–1 GuHCl forms a relatively stable intermediate state under the studied conditions will not be changed by temperature.

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Cover Journal of Thermal Analysis and Calorimetry
Journal of Thermal Analysis and Calorimetry
Print ISSN:
1388-6150
Online ISSN:
1572-8943

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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
Foundation		 1969
Volumes
per Year		 1
Issues
per Year		 24
Founder Akadémiai Kiadó
Founder's
Address		 H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address		 H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher		 Chief Executive Officer, Akadémiai Kiadó
ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)

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