Rheological properties and structure of inulin–whey protein gels |
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| Authors: | Pawel Glibowski |
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| Affiliation: | 1. Top Institute Food and Nutrition, P.O. Box 557, 6700 AN Wageningen, the Netherlands;2. Physics and Physical Chemistry of Foods, Department of Agrotechnology and Food Sciences, Wageningen University, P.O. Box 17, 6700 AA Wageningen, the Netherlands;3. ProtIn Consultancy, Nepveulaan 112 3705LG Zeist, the Netherlands;1. Department of Food Science and Engineering, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai 200240, China;2. Department of Food Processing, Research Institute of Food Science and Technology, Mashhad, Iran;3. Department of Food Nanotechnology, Research Institute of Food Science and Technology, Mashhad, Iran |
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| Abstract: | The rheological properties, structure and synergistic interactions of whey proteins (1–7%) and inulin (20% and 35%) were studied. Gelation of whey proteins was induced with Na+. Inulin was dissolved in preheated whey protein solutions (80 °C, 30 min). Inulin gel formation was strongly affected by whey proteins. The presence of whey proteins at a level allowing for protein gel network formation (7%) significantly increased the G′ and G″ values of the gels. Scanning electron micrographs showed a thick structure for the mixed gel. Whey proteins at low concentrations (1–4%) were not able to form a gel; further, these low concentrations partly or wholly impaired formation of a firm inulin gel. Although interactions between inulin and whey proteins may be concluded from hydrophobicity measurements, the use of an electrophoretic technique did not show any inulin–whey protein complexes. |
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