Capillary electrophoretic behavior of milk proteins in the presence of non-ionic surfactants |
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| Institution: | 1. Engineering Research Center of Optical Instrument and System, Ministry of Education, Shanghai Key Lab of Modern Optical System, University of Shanghai for Science and Technology, No. 516 JunGong Road, Shanghai, 200093, China;2. Department of Clinical Laboratory, Xinhua Hospital, Shanghai Jiao Tong University School of Medicine, 1665 Kongjiang Road, Shanghai, 200092, China;3. Photonics and Bio-medical Research Institute, Department of Physics Faculty of Science, East China University of Science and Technology, No. 130 Meilong Road, Shanghai, 200237, China;4. Department of Applied Physics, Graduate School of Engineering, Osaka University, Yamadaoka Suita-city, Osaka, 565-0871, Japan;1. School of Pharmaceutical Engineering and Life Science, Changzhou University, Changzhou 213164, Jiangsu, People’s Republic of China;2. Department of Biomedical Science, Mercer University School of Medicine, Savannah Campus, Hoskins Building, Room #2209, 4700 Waters Ave., Savannah, GA 31404, USA;3. Advanced Catalysis and Green Manufacturing Collaborative Innovation Center, Changzhou University, Changzhou 213164, Jiangsu, People’s Republic of China;4. Institute of Bioanalytical Chemistry, School of Chemical Engineering, Nanjing University of Science and Technology, No. 200 Xiaolingwei Street, Nanjing 210094, Jiangsu, People’s Republic of China;1. Jiangsu Key Laboratory of New Drug Research and Clinical Pharmacy, Xuzhou Medical University, Xuzhou, Jiangsu 221004, China;2. Department of Bioinformatics, Xuzhou Medical University, Xuzhou, Jiangsu 221004, China;3. Department of Chemistry, Zhejiang University, Hangzhou, Zhejiang 310058, China |
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| Abstract: | The electrophoretic behavior of α-lactalbumin and β-lactoglobulins (A and B) in the presence of non-ionic surfactants was studied by capillary electrophoresis (CE), using a poly(ethylene glycol) coated capillary column. The surfactants (Tween 20, Brij 35 and 78) were used as buffer additives. The separation is based on the difference in the strength of protein–surfactant association complexes, which results in a change of the effective electrophoretic mobility. The modification of the electrophoretic mobilities of proteins was observed and this variation permitted the estimation of the interaction between protein and surfactant. The effect of surfactant type and concentration on the migration behavior of protein in CE is discussed. It is found that the retention behavior of the milk proteins (the α-lactalbumin and the β-lactoglobulins) in CE is very different. The pH of the buffer and the surfactant type influence significantly the protein–surfactant interactions. |
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