Journal of Thermal Analysis and Calorimetry
Volume/Issue:
Volume 102: Issue 2
Thermodynamic investigation of effect of salt concentrations on denatured α-Amylase adsorbed onto a moderately hydrophobic surface
Authors:
X. Feng College of Environment & Chemical Engineering, Xi’an Polytechnic University, Xi’an, 710048 China

Search for other papers by X. Feng in
Current site
Google Scholar
PubMed Close
,
X. Geng College of Environment & Chemical Engineering, Xi’an Polytechnic University, Xi’an, 710048 China

Search for other papers by X. Geng in
Current site
Google Scholar
PubMed Close
,
J. Peng College of Environment & Chemical Engineering, Xi’an Polytechnic University, Xi’an, 710048 China

Search for other papers by J. Peng in
Current site
Google Scholar
PubMed Close
,
H. Hou College of Environment & Chemical Engineering, Xi’an Polytechnic University, Xi’an, 710048 China

Search for other papers by H. Hou in
Current site
Google Scholar
PubMed Close
, and
Q. Bai Institute of Modern Separation Science, Northwest University, Xi’an, 710069 China

Search for other papers by Q. Bai in
Current site
Google Scholar
PubMed Close
Pages:
799–807
Online Publication Date:
10 Dec 2009
Publication Date:
01 Nov 2010
Article Category:
Research Article
DOI:
https://doi.org/10.1007/s10973-009-0611-5
Keywords:
Adsorption; Calorimetry; Thermodynamics; α-Amylase; Protein folding; Hydrophobic surface; Secondary structure
Restricted access

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.

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

To see the editorial board, please visit the website of Springer Nature.

Manuscript Submission: HERE

For subscription options, please visit the website of Springer Nature.

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)

Monthly Content Usage

Abstract Views Full Text Views PDF Downloads
Oct 2024 38 0 0
Nov 2024 7 0 0
Dec 2024 8 0 0
Jan 2025 27 0 0
Feb 2025 17 0 0
Mar 2025 14 0 0
Apr 2025 0 0 0