Effect of polyols on the native structure of α-chymotrypsin: A comparable study

Awanish Kumar, Pankaj Attri, Pannuru Venkatesu

研究成果: ジャーナルへの寄稿学術誌査読

46 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)55-62
ページ数8
ジャーナルThermochimica Acta
536
DOI
出版ステータス出版済み - 5月 20 2012
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • 器械工学
  • 凝縮系物理学
  • 物理化学および理論化学

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