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Relationship between foaming properties and solution properties of protein/nonionic surfactant mixtures
Author(s) -
Wei Xiaofang,
Liu Huizhou
Publication year - 2000
Publication title -
journal of surfactants and detergents
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.349
H-Index - 48
eISSN - 1558-9293
pISSN - 1097-3958
DOI - 10.1007/s11743-000-0148-6
Subject(s) - pulmonary surfactant , chemistry , bovine serum albumin , critical micelle concentration , foaming agent , micelle , molar concentration , chromatography , molar ratio , molecule , nonionic surfactant , chemical engineering , aqueous solution , organic chemistry , biochemistry , porosity , engineering , catalysis
The foaming properties of bovine serum albumin (BSA), in the absence and presence of Triton X‐100 (TX‐100), have been investigated using shaking tests. The results showed that increases in the TX‐100 bulk concentration rapidly reduced both foam height and foam stability at TX‐100 concentrations below about 0.25 mM, but increased foam height and foam stability at TX‐100 concentration above 0.3 mM. The interaction between BSA and TX‐100 has been studied using fluorescence spectroscopy. The surfactant appeared to bind to BSA with a low molar ratio (about one surfactant molecule per protein molecule) at concentrations below the critical micelle concentration (CMC); the binding became weaker at concentrations above the CMC. It was confirmed that protein‐protein or protein‐surfactant interactions had significant influence upon foaming properties of mixed protein/surfactant system.