Comparison of the ability to bind lipids of β-lactoglobulin and serum albumin of milk from ruminant and non-ruminant species

The interaction of sheep, horse, pig, human and guinea-pig whey proteins with fatty acids has been studied. Using gel filtration and autoradiography, it was found that sheep β-lactoglobulin and serum albumin from all species had the ability to bind fatty acids in vitro. Sheep β-lactoglobulin, isolat...

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Bibliographic Details
Published in:Journal of dairy research 1993-02, Vol.60 (1), p.55-63
Main Authors: Pérez, M. Dolores, Puyol, Pilar, Ena, José Manuel, Calvo, Miguel
Format: Article
Language:English
Subjects:
Animals
beta-lactoglobulin
Biological and medical sciences
Cattle
Fatty Acids - metabolism
Food industries
Fundamental and applied biological sciences. Psychology
Guinea Pigs
Horses
Humans
Lactoglobulins - metabolism
Lipid Metabolism
Milk - metabolism
Milk and cheese industries. Ice creams
Milk Proteins - metabolism
milks
Original Articles
Protein Binding
ruminants
Ruminants - metabolism
Serum Albumin - metabolism
Sheep
species differences
Swine
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Summary:The interaction of sheep, horse, pig, human and guinea-pig whey proteins with fatty acids has been studied. Using gel filtration and autoradiography, it was found that sheep β-lactoglobulin and serum albumin from all species had the ability to bind fatty acids in vitro. Sheep β-lactoglobulin, isolated from milk, had ˜ 0·5 mol fatty acids bound per mol monomer protein, and albumin from sheep, horse and pig contained ˜ 4·5, 2·9 and 4·7 mol fatty acids/mol protein respectively. However, β-lactoglobulin from horse and pig milk had neither fatty acids physiologically bound nor the ability to bind them in vitro. Albumin was the only whey protein detected with bound fatty acids in these species as well as in human and guinea pig. This suggests that the ability of ruminant β-lactoglobulin to bind fatty acids was not shared by the same protein of non-ruminants.
ISSN:0022-0299
1469-7629
DOI:10.1017/S0022029900027345