Publisert 2009

Les på engelsk


Tidsskrift : Journal of Agricultural and Food Chemistry , vol. 57 , p. 3563–3570–8 , 2009

Utgiver : American Chemical Society (ACS)

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

Publikasjonstype : Vitenskapelig artikkel

Bidragsytere : Carton, Izaskun; Böcker, Ulrike; Ofstad, Ragni; Sørheim, Oddvin; Kohler, Achim

Sak : 9

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Kjetil Aune


Fourier transform infrared (FT-IR) microspectroscopy and light microscopy were used to study changes in the myofibrillar proteins and microstructure in salmon muscle due to dry salting and smoking. Light microscopy showed that the myofibers of the smoked samples were more shrunken and their shape more irregular and edged than for the nonsmoked samples. FT-IR microspectroscopy showed that salting time mostly contributed in the amide I region, revealing that secondary structural changes of proteins were primarily affected by salting. The main variation in the amide II region was caused by smoking. As it is known that smoke components can react with amino acid side chains and that the contribution of the side chain in the amide II region is larger than that in amide I, it is concluded that the observed differences are due to interactions between carbonyl compounds of smoke and amino acid side chains.