Abstract
For the determination of the binding of heated cow’s milk whey proteins such as β-lactoglobulin to the receptors expressed on immune cells, inhibition ELISA with the soluble form of the receptor for advanced glycation end products (sRAGE) and scavenger receptor class B (CD36) has been successfully used in the past. However, binding to heated and glycated caseins in this read-out system has not been tested. In this study, inhibition ELISA was applied to measure the binding of cow’s milk casein alone, as well as all milk proteins together, which underwent differential heat treatment, to sRAGE and CD36, and we compared those results to a dot blot read out. Moreover, binding to sRAGE and CD36 of differentially heated milk protein was measured before and after in vitro digestion. Casein showed binding to sRAGE and CD36, independent from the heat treatment, in ELISA, while the dot blot showed only binding to high-temperature-heated milk protein, indicating that the binding is not related to processing but to the physicochemical characteristics of the casein. This binding decreased after passage of casein through the intestinal phase.
Highlights
Food Quality & Design Group, Wageningen University & Research Centre, 6708 WG Wageningen, Cell Biology & Immunology, Wageningen University & Research Centre, 6700 AH Wageningen, Wageningen Food & Biobased Research, Wageningen University & Research Centre, 6708 WG Wageningen, Abstract: For the determination of the binding of heated cow’s milk whey proteins such as βlactoglobulin to the receptors expressed on immune cells, inhibition ELISA with the soluble form of the receptor for advanced glycation end products and scavenger receptor class B (CD36) has been successfully used in the past
While whey proteins have been extensively studied regarding their binding to especially the receptor for advanced glycation end products (AGEs) (RAGE), products that contain caseins have not been investigated
No differences were observed in the gastric phase (GP) between samples for sRAGE, while CD36 showed lower binding to LT-milk protein (MP) and higher binding to heated milk protein (HT-MP), compared to Non-treated milk protein (NT-MP)
Summary
Food Quality & Design Group, Wageningen University & Research Centre, 6708 WG Wageningen, Cell Biology & Immunology, Wageningen University & Research Centre, 6700 AH Wageningen, Wageningen Food & Biobased Research, Wageningen University & Research Centre, 6708 WG Wageningen, Abstract: For the determination of the binding of heated cow’s milk whey proteins such as βlactoglobulin to the receptors expressed on immune cells, inhibition ELISA with the soluble form of the receptor for advanced glycation end products (sRAGE) and scavenger receptor class B (CD36) has been successfully used in the past. Inhibition ELISA was applied to measure the binding of cow’s milk casein alone, as well as all milk proteins together, which underwent differential heat treatment, to sRAGE and CD36, and we compared those results to a dot blot read out. Binding to sRAGE and CD36 of differentially heated milk protein was measured before and after in vitro digestion. Casein showed binding to sRAGE and CD36, independent from the heat treatment, in ELISA, while the dot blot showed only binding to high-temperature-heated milk protein, indicating that the binding is not related to processing but to the physicochemical characteristics of the casein. Heated in mixture compared to heating isolated whey proteins [14,15]. Heating of whey proteins in mixture with casein might result in different binding levels to sRAGE compared to their isolated forms. Due to the high binding to the unheated control, further tests were conducted on micellar casein and sodium caseinate
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