Revealing covariance structures in Fourier transform infrared and Raman microspectroscopy spectra:: A study on pork muscle fiber tissue subjected to different processing parameters

被引:79
作者
Bocker, Ulrike
Ofstad, Ragni
Wu, Zhiyun
Bertram, Hanne Christine
Sockalingum, Ganesh D.
Manfait, Michel
Egelandsdal, Bjorg
Kohler, Achim
机构
[1] Norwegian Food Res Inst, Ctr Biospectroscopy & Data Modelling, Matforsk AS, N-1430 As, Norway
[2] Norwegian Univ Life Sci, Dept Chem Biotechnol & Food Sci, N-1432 As, Norway
[3] Res Ctr Foulum, Danish Inst Agr Sci, Dept Food Sci, DK-8830 Tjele, Denmark
[4] Univ Reims, Unite MeDIAN, CNRS, UMR 6142,IFR 53,UFR Pharm, F-51096 Reims, France
[5] ENITIAA INRA, Unite Sensometrie & Chimiometrie, F-44322 Nantes 3, France
关键词
Fourier transform infrared spectroscopy; FT-IR spectroscopy; Raman; microspectroscopy; meat; heating; salting; principal component analysis; multiblock PCA;
D O I
10.1366/000370207782217707
中图分类号
TH7 [仪器、仪表];
学科分类号
0804 ; 080401 ; 081102 ;
摘要
The aim of this study was to investigate the correlation patterns between Fourier transform infrared (FT-IR) and Raman microspectroscopic data obtained from pork muscle tissue, which helped to improve the interpretation and band assignment of the observed spectral features. The pork muscle tissue was subjected to different processing factors, including aging, salting, and heat treatment, in order to induce the necessary degree of variation of the spectra. For comparing the information gained from the two spectroscopic techniques with respect to the experimental design, multiblock principal component analysis (MPCA) was utilized for data analysis. The results showed that both FTIR and Raman spectra were mostly affected by heat treatment, followed by the variation in salt content. Furthermore, it could be observed that IR amide I, II, and III band components appear to be effected to a different degree by brine-salting and heating. FT-IR bands assigned to specific protein secondary structures could be related to different Raman C-C stretching bands. The Raman C-C skeletal stretching bands at 1031, 1061, and 1081 cm(-1) are related to the IR bands indicative of aggregated beta-structures, while the Raman bands at 901 cm(-1) and 934 cm(-1) showed a strong correlation with IR bands assigned to alpha-helical structures. At the same time, the IR band at 1610 cm(-1), which formerly was assigned to tyrosine in spectra originating from pork muscle, did not show a correlation to the strong tyrosine doublet at 827 and 852 cm(-1) found in Raman spectra, leading to the conclusion that the IR band at 1610 cm(-1) found in pork muscle tissue is not originating from tyrosine.
引用
收藏
页码:1032 / 1039
页数:8
相关论文
共 47 条
[1]   FOURIER-TRANSFORM RAMAN AND INFRARED VIBRATIONAL STUDY OF HUMAN SKIN - ASSIGNMENT OF SPECTRAL BANDS [J].
BARRY, BW ;
EDWARDS, HGM ;
WILLIAMS, AC .
JOURNAL OF RAMAN SPECTROSCOPY, 1992, 23 (11) :641-645
[2]   Preliminary investigation of the application of Raman spectroscopy to the prediction of the sensory quality of beef silverside [J].
Beattie, RJ ;
Bell, SJ ;
Farmer, LJ ;
Moss, BW ;
Desmond, PD .
MEAT SCIENCE, 2004, 66 (04) :903-913
[3]   Heat-induced changes in myofibrillar protein structures and myowater of two pork qualities.: A combined FT-IR spectroscopy and low-field NMR relaxometry study [J].
Bertram, HC ;
Kohler, A ;
Böcker, U ;
Ofstad, R ;
Andersen, HJ .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2006, 54 (05) :1740-1746
[4]   Salt-induced changes in pork myofibrillar tissue investigated by FT-IR microspectroscopy and light microscopy [J].
Boecker, Ulrike ;
Ofstad, Ragni ;
Bertram, Hanne Christine ;
Egelandsdal, Bjorg ;
Kohler, Achim .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2006, 54 (18) :6733-6740
[5]   Identification of β-turn and random coil amide III infrared bands for secondary structure estimation of proteins [J].
Cai, SW ;
Singh, BR .
BIOPHYSICAL CHEMISTRY, 1999, 80 (01) :7-20
[6]   LASER RAMAN-STUDY OF INTERNALLY PERFUSED MUSCLE-FIBERS - EFFECT OF MG-2+, ATP AND CA-2+ [J].
CAILLE, JP ;
PIGEONGOSSELIN, M ;
PEZOLET, M .
BIOCHIMICA ET BIOPHYSICA ACTA, 1983, 758 (02) :121-127
[7]   Structural properties of aggregates from frozen stored hake muscle proteins [J].
Careche, M ;
García, ML ;
Herrero, A ;
Solas, MT ;
Carmona, P .
JOURNAL OF FOOD SCIENCE, 2002, 67 (08) :2827-2832
[8]   Structural changes of hake (Merluccius merluccius L.) fillets:: Effects of freezing and frozen storage [J].
Careche, M ;
Herrero, AM ;
Rodriguez-Casado, A ;
Del Mazo, ML ;
Carmona, P .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1999, 47 (03) :952-959
[9]   Structural changes in cod myosin after modification with formaldehyde or frozen storage [J].
Careche, M ;
LiChan, ECY .
JOURNAL OF FOOD SCIENCE, 1997, 62 (04) :717-723
[10]   Importance of frozen storage temperature in the type of aggregation of myofibrillar proteins in cod (Gadus morhua) fillets [J].
Careche, M ;
Del Mazo, ML ;
Torrejón, P ;
Tejada, M .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1998, 46 (04) :1539-1546