Monitoring secondary structural changes in salted and smoked salmon muscle myofiber proteins by FT-IR microspectroscopy.
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.
Carton
Izaskun
I
Matforsk AS, Nofima Food, and Centre for Biospectroscopy and Data Modelling, Osloveien 1, N-1430 As, Norway. izaskun.carton@ehu.es
Böcker
Ulrike
U
Ofstad
Ragni
R
Sørheim
Oddvin
O
Kohler
Achim
A
D000818:Animals; D005511:Food Handling / Q000379:methods*; D009124:Muscle Proteins / Q000737:chemistry*; D009210:Myofibrils / Q000737:chemistry* / Q000648:ultrastructure; D017433:Protein Structure, Secondary; D012474:Salmon; D017747:Seafood / Q000032:analysis; D012906:Smoke; D012965:Sodium Chloride / Q000032:analysis; D017550:Spectroscopy, Fourier Transform Infrared
D009124:Muscle Proteins; D012906:Smoke; D012965:Sodium Chloride