Ethanol stability of casein micelles cross-linked with transglutaminase |
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| Affiliation: | 1. Department of Food and Nutritional Sciences, University College Cork, Ireland;2. NIZO Food Research, PO Box 20, 6710 BA, Ede, The Netherlands;3. Van’t Hoff laboratory for Physical and Colloid Chemistry, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands;1. Kazan Institute of Biochemistry and Biophysics of Kazan Scientific Center of the Russian Academy of Sciences, Kazan, 420111, Russian Federation;2. Kazan (Volga Region) Federal University, Kazan, 420008, Russian Federation;3. BIA, UR 1268, Institut National de la Recherche Agronomique, 44316, Nantes, France;4. Kazan State Power Engineering University, Kazan, 420066, Russian Federation;1. Dairy Science Department, South Dakota State University, Brookings, SD 57007, USA;2. NIZO food research BV, P.O. Box 20, 6710 BA Ede, The Netherlands;1. School of Chemical Sciences, The University of Auckland, Private Bag, 92019, Auckland, New Zealand;2. Institute of Molecular, Cell and Systems Biology, School of Life Sciences, University of Glasgow, Glasgow, G12 8QQ, UK;3. Institute of Fundamental Sciences, Massey University, Palmerston North, New Zealand;4. Chemistry Department, Monash University, Clayton, Victoria 3168, Melbourne, Australia;5. Center for Dairy Research, College of Agriculture and Life Sciences, University of Wisconsin-Madison, 1605 Linden Drive, Madison, USA;6. Shanghai Science Research Center, Chinese Academy of Sciences, Shanghai, 201204, China;7. The Riddet Institute, Palmerston North, New Zealand;1. Institute of Food Technology and Bioprocess Engineering, Technische Universität Dresden, Bergstraße 120, D-01069 Dresden, Germany;2. Department of Chemistry and Food Chemistry, Technische Universität Dresden, Bergstraße 66, D-01069 Dresden, Germany |
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| Abstract: | The influence of transglutaminase (TGase)-induced cross-linking on the ethanol stability of skimmed milk was investigated. The stability of milk against ethanol-induced coagulation increased in sigmoidal fashion with milk pH (5.0–7.5) for all samples; ethanol stability also increased upon incubation (0–24 h) with 0.05 g L−1 TGase at 30 °C. In untreated milk, addition of ethanol induced a collapse of the polyelectrolyte brush of κ-casein on the micelle surface, thereby facilitating micellar aggregation. Dynamic and static light scattering measurements indicated that in TGase-treated milk, the ethanol-induced collapse of the polyelectrolyte brush was far less than in untreated milk, suggesting that the increased ethanol stability of TGase-treated casein micelles is caused by the cross-linking of the polyelectrolyte brush on the micellar surface. |
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