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-   -   [NMR paper] Observations using Phosphorus-31 nuclear magnetic resonance ((31)P-NMR) of structural changes in freeze-thawed hen egg yolk. (http://www.bionmr.com/forum/journal-club-9/observations-using-phosphorus-31-nuclear-magnetic-resonance-31-p-nmr-structural-changes-freeze-thawed-hen-egg-yolk-25270/)

nmrlearner 11-10-2017 05:01 PM

Observations using Phosphorus-31 nuclear magnetic resonance ((31)P-NMR) of structural changes in freeze-thawed hen egg yolk.
 
Observations using Phosphorus-31 nuclear magnetic resonance ((31)P-NMR) of structural changes in freeze-thawed hen egg yolk.

Observations using Phosphorus-31 nuclear magnetic resonance ((31)P-NMR) of structural changes in freeze-thawed hen egg yolk.

Food Chem. 2018 Apr 01;244:169-176

Authors: Wakamatsu H, Handa A, Chiba K

Abstract
Hen egg yolk (EY) has a complicated structure consisting of lipids and proteins, and its structure is deeply related with its functional properties. (31)P-NMR is an efficient technique to non-destructively detect the dynamic behaviour of phospholipids, the main component of bio-membranes. We determined conditions for measuring the (31)P NMR spectra of EY and identified the components. (31)P-NMR was used to detect phosvitin, inorganic phosphate, and lipoprotein as well as structural changes such as granule collapse and freeze-thaw denaturation as signal changes. Freeze-thaw denaturation generated a new denaturation peak. We separated aggregates of LDL from freeze-thawed plasma using centrifugation. TEM and (31)P-NMR observations revealed that the denaturation peak corresponded to LDL aggregates. The (31)P-NMR spectra suggested the formation of multiple forms of LDL aggregates in which the head groups of phospholipid molecules adopt a face-to-face orientation, similar to that observed following the flocculation of lipoproteins or in the lamellar-like structures of phospholipids.


PMID: 29120767 [PubMed - in process]



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