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

journal contribution
posted on 06.12.2017, 00:00 authored by J Rytkonen, K Valkonen, V Virtanen, A Foxwell, Jennelle KydJennelle Kyd, A Cripps, T Karttunen
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.

Funding

Category 1 - Australian Competitive Grants (this includes ARC, NHMRC)

History

Volume

54

Issue

4

Start Page

1500

End Page

1507

Number of Pages

8

eISSN

1520-5118

ISSN

0021-8561

Location

United States

Publisher

American Chemical Society

Language

en-aus

Peer Reviewed

Yes

Open Access

No

External Author Affiliations

Griffith University; Oulun yliopisto; University of Canberra;

Era Eligible

Yes

Journal

Canadian journal of agricultural and food chemistry.