Salt-induced changes in pork myofibrillar tissue investigated by FT-IR microspectroscopy and light microscopy

被引:65
作者
Boecker, Ulrike
Ofstad, Ragni
Bertram, Hanne Christine
Egelandsdal, Bjorg
Kohler, Achim
机构
[1] Matforsk AS, Norwegian Food Res Inst, Ctr Biospect & Data Modelling, N-1430 As, Norway
[2] Norwegian Univ Life Sci, Dept Chem Biotechnol & Food Sci, N-1432 As, Norway
[3] Res Ctr Foulum, Dept Food Sci, Danish Inst Agr Sci, DK-8830 Tjele, Denmark
关键词
FT-IR microspectroscopy; light microscopy; pig muscle; salting; curing;
D O I
10.1021/jf060178q
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
FT-IR microspectroscopy and light microscopy were used to investigate pork muscle musculus semitendinosus samples, taken from three animals, that were subjected to brine salting at different concentrations (0.9, 3, 6, and 9% NaCl). Differences in spectral characteristics and in microstructure were observed in meat from animals differing in initial pH and varying salt concentrations. The FT-IR data displayed changes in the amide I region from 1700 to 1600 cm(-1). This spectral range was analyzed by principal component analysis (PCA) and partial least-squares regression (PLSR). These methods revealed correlations between the spectral data and the different animals, salt content, moisture content, pH value, and myofiber diameter. A shrinking share of R-helical components was related to an increase in salt concentration in the muscle. At the same time, a greater share in nonhydrogenated C=O groups (1668 cm(-1)) was related to an increase in salt concentration in the meat. The share of aggregated,beta-strands differed with respect to the different animals but was not influenced by salt concentration. The meat at higher pHs (> 6) had less aggregated,beta-strands than that at lower pHs (5.6-5.7). It could be demonstrated that simultaneous with changes in microstructure, pH value, salt, and moisture content were alterations in the protein amide I region as measured by FT-IR microspectroscopy, revealing a relationship between these biophysical and chemical parameters and secondary protein structure attributes.
引用
收藏
页码:6733 / 6740
页数:8
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