TY - JOUR
T1 - Effect of polyols on the native structure of α-chymotrypsin
T2 - A comparable study
AU - Kumar, Awanish
AU - Attri, Pankaj
AU - Venkatesu, Pannuru
N1 - Funding Information:
Financial support from the Department of Science and Technology (DST), New Delhi , India through grant No. SR/SI/PC-54/2008 and University Grant Commission (UGC), New Delhi , India grant F. No. 37-404/2009 (SR) is gratefully acknowledged.
PY - 2012/5/20
Y1 - 2012/5/20
N2 - The influence of polyols on the structure and stability of α-chymotrypsin (CT) have been explored by using differential scanning calorimeter (DSC), circular dichroism (CD) and fluorescence spectroscopy. We have predicted the thermodynamic folding properties (transition temperature (T m), enthalpy change (ΔH), heat capacity change (ΔC p) and Gibbs free energy change (ΔG u) from DSC to understand the clear picture of folding studies of CT. All polyols (trehalose, sucrose, sorbitol, and glycerol) acted as enhancers for CT stability, with varying efficacies and efficiencies. The DSC, CD and fluorescence spectral analysis clearly showed the ability of polyols to protect the native structural conformation of enzyme and preventing the unfolding which occurs in the aqueous media. These results explicitly explain that stabilizing polyols are preferentially excluded from the surface of CT, since water has a higher tendency toward favourable interactions with functional groups of the CT than with polyols.
AB - The influence of polyols on the structure and stability of α-chymotrypsin (CT) have been explored by using differential scanning calorimeter (DSC), circular dichroism (CD) and fluorescence spectroscopy. We have predicted the thermodynamic folding properties (transition temperature (T m), enthalpy change (ΔH), heat capacity change (ΔC p) and Gibbs free energy change (ΔG u) from DSC to understand the clear picture of folding studies of CT. All polyols (trehalose, sucrose, sorbitol, and glycerol) acted as enhancers for CT stability, with varying efficacies and efficiencies. The DSC, CD and fluorescence spectral analysis clearly showed the ability of polyols to protect the native structural conformation of enzyme and preventing the unfolding which occurs in the aqueous media. These results explicitly explain that stabilizing polyols are preferentially excluded from the surface of CT, since water has a higher tendency toward favourable interactions with functional groups of the CT than with polyols.
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U2 - 10.1016/j.tca.2012.02.027
DO - 10.1016/j.tca.2012.02.027
M3 - Article
AN - SCOPUS:84862817183
SN - 0040-6031
VL - 536
SP - 55
EP - 62
JO - Thermochimica Acta
JF - Thermochimica Acta
ER -