Title of article :
Effect of polyols on the native structure of α-chymotrypsin: A comparable study
Author/Authors :
Awanish Kumar، نويسنده , , Pankaj Attri، نويسنده , , Pannuru Venkatesu، نويسنده ,
Issue Information :
دوهفته نامه با شماره پیاپی سال 2012
Pages :
8
From page :
55
To page :
62
Abstract :
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 (Tm), enthalpy change (ΔH), heat capacity change (ΔCp) and Gibbs free energy change (ΔGu) 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.
Keywords :
Polyols , ?-chymotrypsin , DSC , Fluorescence spectroscopy , Preferential interactions , CD
Journal title :
Thermochimica Acta
Serial Year :
2012
Journal title :
Thermochimica Acta
Record number :
1200039
Link To Document :
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