Effect of chemical phosphorylation on solubility of buffalo milk proteins |
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| Affiliation: | 1. Dairy Science and Technology Group, Wageningen University, Bornse Weilanden 9, 6708 WG Wageningen, The Netherlands;2. Physics and Physical Chemistry of Foods Group, Wageningen University, Bornse Weilanden 9, 6708 WG Wageningen, The Netherlands;3. Food Technology Centre, Food & Biobased Research, Wageningen University & Research Centre, P.O. Box 17, 6700 AA Wageningen, The Netherlands;4. NIZO Food Research, P.O. Box 20, 6710 BA Ede, The Netherlands;2. Animal Breeding and Genomics Centre, Wageningen University and Research, PO Box 338, 6700 AH Wageningen, the Netherlands;1. School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand;2. School of Biological Sciences, University of Auckland, Auckland, 1010, New Zealand;3. School of Chemical Sciences, University of Auckland, Auckland, 1010, New Zealand;4. MacDiarmid Institute for Advanced Materials and Nanotechnology, Victoria University, Wellington, 6140, New Zealand;5. Riddet Institute, Massey University, Private Bag 11222, Palmerston North, 4442, New Zealand;6. Fonterra Research and Development Centre, Private Bag 11029, Dairy Farm Road, Palmerston North, 4442, New Zealand;1. Department of Food Science and Engineering, College of Food and Pharmaceutical Science, Ningbo University, Ningbo, Zhejiang 315800, China;2. School of Life Sciences and Materials Chemistry, College of Science and Technology Ningbo University, Ningbo, Zhejiang 315800, China;3. Li Dak Sum Marine Biopharmaceutical Research Center, Department of Marine Pharmacy, College of Food and Pharmaceutical Sciences, Ningbo University, Ningbo, Zhejiang 315832, China;1. Key Laboratory of Functional Dairy, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, 100083, China;2. Key Laboratory of Precision Nutrition and Food Quality, Department of Nutrition and Health, China Agricultural University, Beijing, 100089, China |
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| Abstract: | Buffalo milk proteins (casein, co-precipitate or whey protein concentrate) were phosphorylated with phosphorus oxychloride (POCl3) at three different pH values (5.0, 7.0 and 9.0). The solubilities of phosphorylated milk proteins were examined over the pH range 3.0–9.0 in water and ionic (0.1 m NaCl or 10–70 mm Ca2+) systems. The solubilities of buffalo milk proteins decreased at pH 3.0, while there was an increase in the solubilities of casein and co-precipitate near their isoelectric points upon phosphorylation. Solubilities of these phosphorylated milk proteins were pH dependent in 0.1 m NaCl but there was a decrease in their solubilities with increase in calcium ion concentration. This alteration could be due to the shifting of isoionic points of phosphorylated buffalo milk proteins towards acidic pH. |
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