Exploring the thermal stability of α-chymotrypsin in protic ionic liquids

Pankaj Attri, Pannuru Venkatesu

Research output: Contribution to journalArticle

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Abstract

Ammonium based ionic liquids (ILs) are biocompatible co-solvents that stabilize the native state of proteins. Experimentally, we have explored the stability of α-chymotrypsin (CT) in the presence of nine ILs, i.e., diethylammonium acetate (DEAA), diethylammonium hydrogen sulfate (DEAS), diethylammonium dihydrogen phosphate (DEAP), triethylammonium acetate (TEAA), triethylammonium hydrogen sulfate (TEAS), triethylammonium dihydrogen phosphate (TEAP), trimethylammonium acetate (TMAA), trimethylammonium hydrogen sulfate (TMAS), trimethylammonium dihydrogen phosphate (TMAP). Thermodynamic folding properties such as transition temperature (Tm), Gibbs free energy change of unfolding (ΔGU), enthalpy change (ΔH) and heat capacity change (ΔCp) of CT in ILs are obtained by fluorescence spectra analysis. Fluorescence and circular dichroism (CD) spectroscopy experiments were performed to probe CT stabilization and structural changes in the presence of ILs. Our experimental results suggest that the ILs act as stabilizers for the CT structure and the stability of CT depends on the structural arrangement of the ions of ILs. Our experimental results reveal that ILs (DEAA, DEAS and DEAP) having more hydrophobic ammonium cations [DEA +] are weak stabilizers for CT, while trimethyl ammonium cations [TMA+] ILs having small alkyl chain length such as TMAA, TMAS and TMAP are strong stabilizers and therefore more biocompatible for the native structure of CT.

Original languageEnglish
Pages (from-to)462-470
Number of pages9
JournalProcess Biochemistry
Volume48
Issue number3
DOIs
Publication statusPublished - Mar 1 2013

Fingerprint

Ionic Liquids
Chymotrypsin
Ionic liquids
Thermodynamic stability
Hot Temperature
Sulfates
Hydrogen
Phosphates
Acetates
Ammonium Compounds
Cations
Spectrum Analysis
Fluorescence
Positive ions
Circular dichroism spectroscopy
Transition Temperature
Gibbs free energy
Circular Dichroism
Chain length
Thermodynamics

All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology

Cite this

Exploring the thermal stability of α-chymotrypsin in protic ionic liquids. / Attri, Pankaj; Venkatesu, Pannuru.

In: Process Biochemistry, Vol. 48, No. 3, 01.03.2013, p. 462-470.

Research output: Contribution to journalArticle

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