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

被引：46

作者：

Carton, Izaskun ^{[1
,2
,3
]}

Bocker, Ulrike ^{[1
,2
]}

Ofstad, Ragni ^{[1
,2
]}

Sorheim, Oddvin ^{[1
,2
]}

Kohler, Achim ^{[1
,2
,4
,5
]}

机构：

[1] Matforsk AS, Nofima Food, N-1430 As, Norway

[2] Ctr Biospect & Data Modelling, N-1430 As, Norway

[3] Univ Basque Country, Fac Pharm, Vitoria 01006, Spain

[4] Norwegian Univ Life Sci, Ctr Integrat Genet, CIGENE, N-1432 As, Norway

[5] Norwegian Univ Life Sci, Dept Math Sci & Technol, N-1432 As, Norway

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 2009年 / 57卷 / 09期

关键词：

FT-IR microspectroscopy; myofibrillar proteins; salmon; salting; smoking; TRANSFORM INFRARED MICROSPECTROSCOPY; FARMED ATLANTIC SALMON; LISTERIA-MONOCYTOGENES; H-1-NMR RELAXOMETRY; LIGHT-MICROSCOPY; SENSORY QUALITY; PORK QUALITIES; BEEF LOIN; SALAR L; SPECTROSCOPY;

D O I：

10.1021/jf803668e

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

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.

引用

页码：3563 / 3570

页数：8

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