2013
DOI: 10.1039/c3cp44299c
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Thermal unfolding and refolding of lysozyme in deep eutectic solvents and their aqueous dilutions

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Cited by 125 publications
(137 citation statements)
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“…Several factors including hydrophobicity, solvent polarity and hydrogen bond characteristics of ILs can affect separately or together the protein stability and activity (Weingartner et al 2012). Similarly, the concentration of DESs in an aqueous solution had significant effect on the unfolding and refolding process of the enzyme, which could be determined by spectroscopy technologies such as intrinsic fluorescence and CD spectroscopy (Esquembre et al 2013). The two methods can effectively estimate the folded degree of proteins compared to the native-like secondary and tertiary structures.…”
Section: Influence Of Dess On Biocatalysismentioning
confidence: 99%
See 1 more Smart Citation
“…Several factors including hydrophobicity, solvent polarity and hydrogen bond characteristics of ILs can affect separately or together the protein stability and activity (Weingartner et al 2012). Similarly, the concentration of DESs in an aqueous solution had significant effect on the unfolding and refolding process of the enzyme, which could be determined by spectroscopy technologies such as intrinsic fluorescence and CD spectroscopy (Esquembre et al 2013). The two methods can effectively estimate the folded degree of proteins compared to the native-like secondary and tertiary structures.…”
Section: Influence Of Dess On Biocatalysismentioning
confidence: 99%
“…A redshift of the fluorescence emission spectra of tryptophan residues in lysozyme was observed when tryptophan side chain was exposed to a polar surrounding of water molecules. In neat ChCl/U and ChCl/Gly solution, the emission maximum of lysozyme shifted from 335 nm (observed in buffer) to 332 and 329 nm, respectively (Esquembre et al 2013). However, higher concentration of DESs can cause the irreversible unfolding of lysozyme at high temperatures.…”
Section: Influence Of Dess On Biocatalysismentioning
confidence: 99%
“…The eutectic mixture melts as low as 12°C. Lysozyme dissolved in DES retains enzyme activity (32). Because DES enhances the solubility of biomolecules, it has been used for preclinical studies (33).…”
Section: Introductionmentioning
confidence: 99%
“…At 20°C, the highest fluorescence intensity was observed and the k max was located at 340.6 nm with k ex = 295 (Fig. 1A), suggesting that the most tryptophan residues were located in relatively hydrophobic environments in apo-CP43 (Lakowicz and Masters 2008;Esquembre et al 2013;Drake and Hoops 2014). However, the k max is not obviously shifted with the elevated temperature.…”
Section: Resultsmentioning
confidence: 97%
“…The ratio increases sharply from 68 to 71°C and then slowly with the increasing temperature. The synchronous fluorescence spectra (Dk = 15) indicated that there existed the change in the hydrophobicity around the tyrosine residues and it is gradually increasing with the elevated temperature (Samuel et al 2000;Esquembre et al 2013; Drake and Hoops 2014). These results above indicated that high-temperature treatment disrupted the substructures around both of the tryptophan and tyrosine residues in apo-CP43, especially above 40°C, and the heat-induced structural changes were different in the polarity and hydrophobicity around tryptophan and tyrosine residues.…”
Section: Resultsmentioning
confidence: 99%