Effects of heat and β-lactoglobulin on distribution of fluorescently labeled tissue- and urokinase-type plasminogen activators in a model milk system |
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| Affiliation: | 1. Key Laboratory of Functional Dairy, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, PR China;2. Beijing Laboratory for Food Quality and Safety, Beijing, PR China;3. Beijing Higher Institution Engineering Research Center of Animal Product, Beijing, PR China;1. Arla Foods Strategic Innovation Centre, Rørdrumvej 2, DK-8220 Brabrand, Denmark;2. Aarhus University, Dept. of Food Science, Faculty of Science and Technology, Blichers Allé 20, DK-8830 Tjele, Denmark;3. Arla Foods Strategic Innovation Centre, Lindhagensgatan 126, SE-10546 Stockholm, Sweden;4. University of Copenhagen, Department of Food Science, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark;5. Dept of Food Technology, Engineering and Nutrition, Lund University, SE-22100 Lund, Sweden;1. Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Food Science & Nutritional Engineering, China Agricultural University, Beijing, China;2. Beijing Laboratory for Food Quality and Safety, Beijing Higher Institution Engineering Research Center of Animal Product, China Agricultural University, Beijing, China;3. Yunnan Huangshi Lesson Dairy Co. Ltd, Food Industrial Park, Dali Town, Yunnan, China;1. Fonterra Research and Development Centre, Private Bag 11029, Palmerston North 4442, New Zealand;2. Massey Institute of Food Science and Technology, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand;3. Dairy Foods Research and Development, Land O''Lakes, Inc., MN, USA |
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| Abstract: | A fluorescent labeling method was developed to determine the effects of heat and β-lactoglobulin (BLG) on the concentration distribution of added fluorescently labeled tissue-type (tPA-647) and urokinase-type (uPA-546) plasminogen activators (PAs) in a model milk system. Prior to heating, the majority of the added PAs (87% of tPA-647, 72% of uPA-546) became associated with casein micelles and could be dissociated by acidification or NaCl. Addition of 0.5% BLG to the unheated system had no significant effect on the distribution of PAs. Heat-induced binding of uPA-546 to micelles was shown by an increase of uPA-546 from 72% to 88% or 95% in the micelle fraction of systems without or with BLG, respectively. Although heat alone had little effect on the total amount of tPA-647 associated with caseins (88%), addition of BLG to a heated system shifted 32% of the tPA-647 to a non-sedimentable casein fraction. After heating, casein–PA interactions became more complex. |
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