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Publisert 2006

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Publikasjonsdetaljer

Tidsskrift : Journal of Agricultural and Food Chemistry , vol. 54 , p. 8589–8597 , 2006

Utgiver : American Chemical Society (ACS)

Internasjonale standardnummer :
Trykt : 0021-8561
Elektronisk : 1520-5118

Publikasjonstype : Vitenskapelig artikkel

Bidragsytere : Wu, Zhiyun; Bertram, Hanne Christine; Kohler, Achim; Böcker, Ulrike; Ofstad, Ragni; Andersen, Henrik J.

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Kjetil Aune
Bibliotekleder
kjetil.aune@nofima.no

Sammendrag

Fourier transform infrared (FT-IR) microspectroscopy and low-field (LF) proton NMR transverse relaxation measurements were used to study the changes in protein secondary structure and water distribution as a consequence of aging (1 day and 14 days) followed by salting (3%, 6%, and 9% NaCl) and cooking (65 degrees C). An enhanced water uptake and increased proton NMR relaxation times after salting were observed in aged meat (14 days) compared with nonaged meat (1 day). FT-IR bands revealed that salting induced an increase in native beta-sheet structure while aging triggered an increase in native alpha-helical structure before cooking, which could explain the effects of aging and salting on water distribution and water uptake. Moreover, the decrease in T-2 relaxation times and loss of water upon cooking were attributed to an increase in aggregated beta-sheet structures and a simultaneous decrease in native protein structures. Finally, aging increased the cooking loss and subsequently decreased the final yield, which corresponded to a further decrease in T-2 relaxation times in aged meat upon cooking. However, salting weakened the effect of aging on the final yield, which is consistent with the increased T-2 relaxation times upon salting for aged meat after cooking and the weaker effect of aging on protein secondary structural changes for samples treated with high salt concentration. The present study reveals that changes in water distribution during aging, salting, and cooking are not only due to the accepted causal connection, i.e., proteolytic degradation of myofibrillar structures, change in electrostatic repulsion, and dissolution and denaturation of proteins, but also dynamic changes in specific protein secondary structures.

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