4.7 Article

Fat globules selected from whole milk according to their size: Different compositions and structure of the biomembrane, revealing sphingomyelin-rich domains

Journal

FOOD CHEMISTRY
Volume 125, Issue 2, Pages 355-368

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2010.09.005

Keywords

Milk fat globule membrane; Phospholipid; Sphingolipid; Lipid raft; Microfiltration

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Milk fat globules are unique delivery systems for biologically active molecules in the gastrointestinal tract. However, their properties have not yet been fully investigated. In this study, we performed a comparative analysis of the polar lipid and fatty acid compositions of milk fat globules as a function of their size and investigated the structure of the milk fat globule membrane (MFGM). An optimised process of microfiltration was used to select the small milk fat globule (SMFG; 1.6 mu m) fractions and the large milk fat globule (LMFG; 6.6 mu m) fractions from the same initial whole milks (4.2 mu m). The SMFG-fractions contained significantly (i) higher amounts of polar lipids, 8.9 +/- 0.9 vs 2.7 +/- 0.3 mg/g fat for LMFG-fractions and 6.3 +/- 0.5 mg/g fat for whole milks, (ii) lower relative proportions of phosphatidylcholine and sphingomyelin in the MFGM, (iii) higher amounts of C12:0, C14:0, C16:0, C18:1 trans, C18:2 c9 tr11, and lower amounts of C18:0 and C18:1 c9 than did LMFG-fractions and whole milks. Whatever the size of native milk fat globules, the biophysical characterisation performed in-situ, using confocal laser scanning microscopy, showed heterogeneities in the MFGM. The lateral segregation of sphingomyelin in rigid liquid-ordered domains, surrounded by the fluid matrix of glycerophospholipids in the liquid-disordered phase, was revealed. The heterogeneous distribution of glycolipids and glycoproteins was also observed in the MFGM. A new model for the structure of the MFGM is proposed and discussed. The physical, chemical and biological consequences, (i) of the differences in milk fat globule compositions according to their size and (ii) of the specific structure of the MFGM due to sphingomyelin remain to be elucidated. (C) 2010 Elsevier Ltd All rights reserved.

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