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Enterocyte and M-Cell Transport of Native and Heat-Denatured Bovine β-Lactoglobulin: Significance of Heat Denaturation
The three-dimensional structure, digestibility, and immunological properties of bovine β-lactoglobulin (β-lg) 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-lg, the transport...
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Published in: | Journal of agricultural and food chemistry 2006-02, Vol.54 (4), p.1500-1507 |
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Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | The three-dimensional structure, digestibility, and immunological properties of bovine β-lactoglobulin (β-lg) 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-lg, the transport of native and heat-denatured bovine β-lg was investigated in experimental cell models using Caco-2 cells and M cells. Transport of β-lg 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-lg more efficiently than they did heat-denatured β-lg. In addition, M cells transported native β-lg more than Caco-2 cells. Transport of native and heat-denatured β-lg was transcellular. The electrophoretic data also suggest that heat-denatured β-lg may have degraded more than native β-lg during the transport. Keywords: β-Lactoglobulin; M cell; Caco-2 cell; heat denaturation; transport |
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ISSN: | 0021-8561 1520-5118 |
DOI: | 10.1021/jf052309d |