Dilational rheology of different globular protein with imidazolium-based ionic liquid surfactant adsorption layer at the decane/water interface
文献类型: 外文期刊
第一作者: Zhou, Zhao-Lu
作者: Zhou, Zhao-Lu;Zheng, Li;Huang, Qi-Liang;Du, Feng-Pei
作者机构:
关键词: Imidazolium-based ionic liquid surfactant;Dilational rheology;Interfacial tension relaxation;Lysozyme;Bovine serum albumin
期刊名称:JOURNAL OF MOLECULAR LIQUIDS ( 影响因子:6.165; 五年影响因子:5.642 )
ISSN: 0167-7322
年卷期: 2017 年 233 卷
页码:
收录情况: SCI
摘要: This contribution is concerned with the imidazolium-based ionic liquid surfactant being considered potential amphiphilic molecules. The interfacial dilational rheology of solutions of globular proteins (lysozyme and bovine serum albumin (BSA)) with imidazolium-based ionic liquid surfactant (1-dodecyl-3-methyl imidazolium bromide ([C(12)mim]Br)) have been measured as a function of the surfactant concentration, interface lifetime and interfacial pressure. The dynamic interfacial dilational modulus of lysozyme/[C(12)mim]Br solutions are always monotonous, but that of the BSA/[C(12)mim]Br solutions become nonmonotonous indicating the destruction of the protein structure. One can assume that some lysozyme molecules desorb from interface due to competitive of free [C(12)mim]Br molecules for lysozyme/[C(12)mim]Br solution with [C(12)mim]Br concentration increasing, however, BSA molecules unfolding of compact globule have been subject to conformational changes so that it can give space for more [C(12)mim]Br molecules to co-adsorb. This aimed to provide more theoretical information for practical applications of imidazolium-based ionic liquid surfactant. (C) 2017 Elsevier B.V. All rights reserved.
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