Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/227423

Title

Enterocyte and M-cell transport of native and heat-denatured bovine beta-lactoglobulin: significance of heat denaturation

Author(s)

Rytkonen, Jani;  Valkonen, Kaija H.;  Virtanen, Vesa;  Foxwell, Ruth A.;  Kyd, Jennelle M.;  Cripps, Allan W.;  Karttunen, Tuomo J.

Abstract

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

Source

Journal of Agricultural and Food Chemistry, Vol. 54, no. 4 (Jan 2006), pp. 1500-1507

Publication year

2006

FOR Code(s)

03 Chemical Sciences;  07 Agricultural and Veterinary Sciences;  09 Engineering

Keyword(s)

Beta-lactoglobulin;  Biological transport;  Caco-2 cells;  Enterocytes;  Epithelial cells;  Heat denaturation;  Lactoglobulins;  M cells;  Metabolism;  Protein denaturation;  Trypsin

Publisher

American Chemical Society

ISSN

0021-8561

Publisher URL

http://dx.doi.org/10.1021/jf052309d

Copyright

Copyright © 2006 American Chemical Society.

Peer reviewed