Comparison of the ability to bind lipids of beta-lactoglobulin and serum albumin of milk from ruminant and non-ruminant species.
Abstract: 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 beta-lactoglobulin and serum albumin from all species had the ability to bind fatty acids in vitro. Sheep beta-lactoglobulin, isolated from milk, had approximately 0.5 mol fatty acids bound per mol monomer protein, and albumin from sheep, horse and pig contained approximately 4.5, 2.9 and 4.7 mol fatty acids/mol protein respectively. However, beta-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 beta-lactoglobulin to bind fatty acids was not shared by the same protein of non-ruminants.
Publication Date: 1993-02-01 PubMed ID: 8436666DOI: 10.1017/s0022029900027345Google Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research investigated how proteins found in milk from different species (sheep, horse, pig, human, guinea pig) interact with fatty acids. Specifically, it explored the protein’s ability to bind with fatty acids, discovering that this ability varies between species.
Research Objectives and Methods
- The main objective of the study was to compare the fatty acid binding capabilities of two milk proteins (beta-lactoglobulin and serum albumin) from various animal species.
- The researchers used gel filtration and autoradiography to study this interaction.
Findings: Sheep Milk
- It was found that in sheep milk both the beta-lactoglobulin protein and the serum albumin have the ability to bind with fatty acids.
- Specifically, approximately 0.5 moles of fatty acids were bound per mole of beta-lactoglobulin, and the albumin protein contained almost 3-5 times that amount.
Findings: Horse and Pig Milk
- In contrast, the beta-lactoglobulin protein from horse and pig milk was found to have neither naturally occurring fatty acids bound nor the ability to bind with them in laboratory conditions.
- For these species, albumin was the only milk protein that showed an ability to bind with fatty acids.
Findings: Human and Guinea Pig Milk
- In human and guinea pig milk, similar to the findings in horse and pig milk, albumin was the only protein that had the ability to bind with fatty acids.
Conclusion
- The study concludes that the ability of the beta-lactoglobulin protein to bind with fatty acids, which is found in ruminant animals like sheep, is not a characteristic shared with the same protein in non-ruminants like horses, pigs, humans, and guinea pigs.
The research provides valuable insights on the different metabolic processes and adaptations across various species, particularly in the interaction of milk proteins and fats. This understanding can also have implications in human food science and nutrition, as milk and its proteins are commonly consumed in various forms.
Cite This Article
APA
Pérez MD, Puyol P, Ena JM, Calvo M.
(1993).
Comparison of the ability to bind lipids of beta-lactoglobulin and serum albumin of milk from ruminant and non-ruminant species.
J Dairy Res, 60(1), 55-63.
https://doi.org/10.1017/s0022029900027345 Publication
Researcher Affiliations
- Tecnología y Bioquímica de los Alimentos, Facultad de Veterinaria, Universidad de Zaragoza, España.
MeSH Terms
- Animals
- Cattle
- Fatty Acids / metabolism
- Guinea Pigs
- Horses
- Humans
- Lactoglobulins / metabolism
- Lipid Metabolism
- Milk / metabolism
- Milk Proteins / metabolism
- Protein Binding
- Ruminants / metabolism
- Serum Albumin / metabolism
- Sheep
- Swine
Citations
This article has been cited 3 times.- Sawyer L. β-Lactoglobulin and Glycodelin: Two Sides of the Same Coin?. Front Physiol 2021;12:678080.
- Le Maux S, Bouhallab S, Giblin L, Brodkorb A, Croguennec T. Bovine β-lactoglobulin/fatty acid complexes: binding, structural, and biological properties.. Dairy Sci Technol 2014;94(5):409-426.
- Mercadante D, Melton LD, Norris GE, Loo TS, Williams MA, Dobson RC, Jameson GB. Bovine β-lactoglobulin is dimeric under imitative physiological conditions: dissociation equilibrium and rate constants over the pH range of 2.5-7.5.. Biophys J 2012 Jul 18;103(2):303-12.
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