Scientific Publications with referee

Monitoring Secondary Structural Changes in Salted and Smoked Salmon Muscle Myofiber Proteins by FT-IR Microspectroscopy.

 

Facts

Year 2009
Abstract 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.
Reference Carton, I., Böcker, U., Ofstad, R., Sørheim, O., Kohler, A. 2009. Monitoring Secondary Structural Changes in Salted and Smoked Salmon Muscle Myofiber Proteins by FT-IR Microspectroscopy. Journal of Agricultural and Food Chemistry, Vol 57, pp 3563-3570.
Publisher Journal of Agricultural and Food Chemistry,

Related persons

  • Ulrike Böcker

    Research Scientist

    Phone: +47 64970294

  • Ragni Ofstad

    Research Director, Raw materials and Process Optimisation

    Phone: +47 64970293

    Cellphone: +47 90 59 29 81

  • Oddvin Sørheim

    Senior Research Technologist

    Phone: +47 64970239

    Cellphone: +47 900 15 436

  • Achim Kohler

    Research Scientist

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    Cellphone: +47 901 80 765