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The stability of α‐chymotrypsin in the ionic liquid, 1‐ethyl‐3‐methyl‐imidizolium bis[(trifluoromethyl)sulfonyl]amide ([emim][NTf₂]), was studied at 30 and 50°C and compared with the stability in other liquid media, such as water, 3 M sorbitol, and 1‐propanol. The kinetic analysis of the enzyme stability pointed to the clear denaturative effect of 1‐propanol, while both 3M sorbitol and [emim][NTf₂] displayed a strong stabilizing power. For the first time, it is shown that enzyme stabilization by ionic liquids seems to be related to the associated structural changes of the protein that can be observed by differential scanning calorimetry (DSC) and fluorescence and circular dichroism (CD). The [emim][NTf₂] enhanced both the melting temperature and heat capacity of the enzyme compared to the other media assayed. The fluorescence spectra clearly showed the ability of [emim][NTf₂] to compact the native structural …