Development of a low resolution (1)H NMR spectroscopic technique for the study of matrix mobility in fresh and freeze-thawed hen egg yolk.
Food Chem. 2016 Aug 1;204:159-66
Authors: Au C, Wang T, Acevedo NC
Abstract
Three experiments were conducted in developing a low resolution proton nuclear magnetic resonance ((1)H NMR) spectroscopic technique to study matrix mobility in fresh and freeze-thawed gelled yolk. The Carr-Purcell-Meiboom-Gill (CPMG) sequence was used to measure spin-spin relaxation times of proton pools representing major yolk constituents. A component identification test distinguished 3-4 pools. The least mobile pool was assigned to proteins, protein-lipid and protein-water interactions, and the most mobile to unbound water. The remaining pools were assigned to lipids, lipid-protein and lipid-water interactions. A stability test indicated that yolk had varied matrix mobility within the same sample across five days of refrigeration storage. A reproducibility test demonstrated high repeatability of fresh yolk measurements, but significant differences (p
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Development of a low resolution (1)H NMR spectroscopic technique for the study of matrix mobility in fresh and freeze-thawed hen egg yolk.
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