Enzymatic Activity and Thermal Stability of Metallo Proteins in Hydrated Ionic Liquids
Enzymatic Activity and Thermal Stability of Metallo Proteins in Hydrated Ionic Liquids
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DOI：
10.1002/bip.21526
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发表时间：
2010-12-01
期刊：
影响因子：
2.9
通讯作者：
Ohno, Hiroyuki
中科院分区：
文献类型：
--
作者：
Fujita, Kyoko;Ohno, Hiroyuki
Hydrated choline dihydrogen phosphate (Hy[ch][dhp]) containing 30 wt% water was investigated as a novel protein solvent. The Hy[ch][dhp] dissolved some metallo proteins (cytochrome c, peroxidase, ascorbate oxidase, azurin, pseudoazurin and fructose dehydrogenase) without any modification. These proteins retained the surroundings of the active site after dissolution in Hy[ch][dhp]. Some metallo proteins were found to retain their activity in the Hy[ch][dhp]. (C) 2010 Wiley Periodicals, Inc. Biopolymers 93: 1093-1099, 2010.
