作者: Chong Cao , Li-Dong Cao , Qi-Liang Huang , Feng-Pei Du
DOI: 10.1080/01932691.2017.1281143
关键词: Ionic liquid 、 Inorganic chemistry 、 Chemistry 、 Molecule 、 Decane 、 Chemical engineering 、 Pulmonary surfactant 、 Adsorption 、 Surface tension 、 Hydrophobic effect 、 Protein adsorption
摘要: ABSTRACTThe interfacial behavior of β-casein and BSA solutions have been investigated in the presence imidazolium-based ionic liquid surfactant ([C14mim]Br) at decane/water interface with oscillating drop tension relaxation measurements. Both electrostatic hydrophobic interaction between protein [C14mim]Br played crucial roles as concentration increases. Furthermore, it was found that dilational rheology parameters provided information adsorbed layers structure, dynamics properties depend on bulk concentration. Moreover, increasing, layer subject to conformational changes where gave space molecules form co-adsorb; for BSA/[C14mim]Br solutions, globule deformed then co-adsorb interface. These results will contribute elucidation ...