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

Published online by Cambridge University Press:  01 June 2009

M. Dolores Pérez ,
Pilar Puyol ,
José Manuel Ena  and
Miguel Calvo
M. Dolores Pérez
Affiliation:
Tecnología y Bioquímica de los Alimentos, Facultad de Veterinaria, Universidad de Zaragoza, Miguel Servet 177, 50013 Zaragoza, España
Pilar Puyol
Affiliation:
Tecnología y Bioquímica de los Alimentos, Facultad de Veterinaria, Universidad de Zaragoza, Miguel Servet 177, 50013 Zaragoza, España
José Manuel Ena
Affiliation:
Tecnología y Bioquímica de los Alimentos, Facultad de Veterinaria, Universidad de Zaragoza, Miguel Servet 177, 50013 Zaragoza, España
Miguel Calvo*
Affiliation:
Tecnología y Bioquímica de los Alimentos, Facultad de Veterinaria, Universidad de Zaragoza, Miguel Servet 177, 50013 Zaragoza, España
*
*For correspondence.
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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.

Type
Original Articles
Information
Journal of Dairy Research , Volume 60 , Issue 1 , February 1993 , pp. 55 - 63
Copyright
Copyright © Proprietors of Journal of Dairy Research 1993

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References

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