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
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

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
Jan 2024 15 0 2
Feb 2024 7 1 0
Mar 2024 1 0 0
Apr 2024 14 0 0
May 2024 5 0 0
Jun 2024 2 0 0
Jul 2024 4 0 0