Development of a low resolution 1H NMR spectroscopic technique for the study of matrix mobility in fresh and freeze-thawed hen egg yolk
2016
Au, Carmen | Wang, Tong | Acevedo, Nuria C.
Three experiments were conducted in developing a low resolution proton nuclear magnetic resonance (1H 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<0.05) were found within gelled yolk samples. This research determined that 1H NMR spectroscopy, a non-destructive technique, can identify yolk components and detect changes in the matrix.
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