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Home List of Titles Enterocyte and M-cell transport of native and heat-denatured bovine beta-lactoglobulin: significance of heat denaturation
Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/227423
- Enterocyte and M-cell transport of native and heat-denatured bovine beta-lactoglobulin: significance of heat denaturation
- Rytkonen, Jani; Valkonen, Kaija H.; Virtanen, Vesa; Foxwell, Ruth A.; Kyd, Jennelle M.; Cripps, Allan W.; Karttunen, Tuomo J.
- The three-dimensional structure, digestibility, and immunological properties of bovine β-lactoglobulin (β-Ig) are modified by heat treatments used in processing of liquid milk products. Because it is not known if such treatments also modify the intestinal transport properties of β-Ig, the transport of native and heat-denatured bovine β-Ig was investigated in experimental cell models using Caco-2 cells and M cells. Transport of β-Ig labeled with a fluorescent marker was followed with fluorometric measurements, electrophoretic analyses, and fluorescence microscopy. The data show that both cell types transported native β-Ig more efficiently than they did heat-denatured β-Ig. In addition, M cells transported native β-Ig more than Caco-2 cells. Transport of native and heat-denatured β-Ig was transcellular. The electrophoretic data also suggest that heat-denatured β-Ig may have degraded more than native β-Ig during the transport.
- Publication type
- Journal article
- Journal of Agricultural and Food Chemistry, Vol. 54, no. 4 (Jan 2006), pp. 1500-1507
- Publication year
- FOR Code(s)
- 03 Chemical Sciences; 07 Agricultural and Veterinary Sciences; 09 Engineering
- Beta-lactoglobulin; Biological transport; Caco-2 cells; Enterocytes; Epithelial cells; Heat denaturation; Lactoglobulins; M cells; Metabolism; Protein denaturation; Trypsin
- American Chemical Society
- Publisher URL
- Copyright © 2006 American Chemical Society.
- Peer reviewed