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Thermal stability of proteins in the presence of aprotic ionic liquids 被引量:1
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作者 Hidetaka Noritomi ken minamisawa +1 位作者 Reo Kamiya Satoru Kato 《Journal of Biomedical Science and Engineering》 2011年第2期94-99,共6页
Thermal stability of lysozyme dissolved in aqueous solutions was examined in the presence of water-miscible aprotic ionic liquids consisting of 1-ethyl-3-methylimidazolium cation and several kinds of anions. Addition ... Thermal stability of lysozyme dissolved in aqueous solutions was examined in the presence of water-miscible aprotic ionic liquids consisting of 1-ethyl-3-methylimidazolium cation and several kinds of anions. Addition of ionic liquids to an aqueous solution containing lysozyme prevented unfolded proteins from aggregating irreversibly at high temperatures. The thermal denaturation curve of lysozyme with ionic liquids was entirely shifted to higher temperature, compared with that without ionic liquids. The remaining activity of lysozyme after the heat treatment was markedly dependent upon the kind and concentration of ionic liquids. The remaining activi-ties of lysozyme with 1.5 M 1-ethyl-3-methylimida-zolium tetrafluoroborate ([emim][BF4]) and 0.1 M 1-ethyl-3-methylimidazolium trifluoromethanesulfonate ([emim][Tf]) exhibited 88 and 68% after the heat treatment at 90oC for 30 min, respectively, although that without ionic liquids was perfectly lost. 展开更多
关键词 Thermal Stability LYSOZYME IONIC LIQUID REMAINING ACTIVITY
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