Monitoring of denaturation processes in aged beef loin by Fourier transform infrared microspectroscopy.

We present the results of a Fourier transform infrared (FT-IR) microspectroscopic study using conventional FT-IR microscopy and FT-IR imaging to detect the denaturation process during four different heating temperatures (raw, 45, 60, and 70 degrees C) spatially resolved in bovine cryosections from longissimus dorsi muscle. FT-IR imaging, employing a focal plane array detector, which allowed the simultaneous collection of spectra at 4096 pixels, enabled the investigation of the heat-induced changes in the two major meat constituents, i.e., myofibrillar and connective tissue proteins, spatially resolved. The infrared spectra of both compounds revealed that the major spectral changes involved an increase in beta-sheet and a decrease in alpha-helical structures, which appeared to be much more pronounced for the myofibers than for the connective tissue. These conformational changes could be correlated to the denaturation of the major meat proteins, such as myosin, actin, and collagen.

[1]  Peter Lasch,et al.  Molecular Changes of Preclinical Scrapie Can Be Detected by Infrared Spectroscopy , 2002, The Journal of Neuroscience.

[2]  Boiana O. Budevska,et al.  Application of Multivariate Curve Resolution for Analysis of FT-IR Microspectroscopic Images of in Situ Plant Tissue , 2003, Applied spectroscopy.

[3]  J. Bandekar,et al.  Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. , 1986, Advances in protein chemistry.

[4]  Robert G. Messerschmidt,et al.  Infrared microspectroscopy : theory and applications , 1988 .

[5]  E. Neil Lewis,et al.  Uncooled Barium Strontium Titanium Focal Plane Array Detection for Mid-Infrared Fourier Transform Spectroscopic Imaging , 2000 .

[6]  Harald Labischinski,et al.  Elaboration of a procedure for identification of bacteria using Fourier-Transform IR spectral libraries: a stepwise correlation approach , 1991 .

[7]  K. Palka.  The influence of post-mortem ageing and roasting on the microstructure, texture and collagen solubility of bovine semitendinosus muscle. , 2003, Meat science.

[8]  T. Tsuchiya,et al.  Differential scanning calorimetric studies on thermal behaviors of myofibrillar proteins. , 1985 .

[9]  H. Fabian,et al.  Fourier Transform Infrared Spectroscopy in Peptide and Protein Analysis , 2006 .

[10]  H. Martens,et al.  Variable Selection in near Infrared Spectroscopy Based on Significance Testing in Partial Least Squares Regression , 2000 .

[11]  M. Stone.  Cross‐Validatory Choice and Assessment of Statistical Predictions , 1976 .

[12]  R. C. Reeder,et al.  Fourier transform spectroscopic imaging using an infrared focal-plane array detector. , 1995, Analytical chemistry.

[13]  P. Wilding,et al.  Differential scanning calorimetric study of muscle and its proteins: myosin and its subfragments. , 1984, Journal of the science of food and agriculture.

[14]  R. L. Olsen,et al.  Liquid loss as effected by Post mortem ultrastructural changes in fish muscle : Cod (Gadus morhua L) and Salmon (Salmo salar) , 1996 .

[15]  A. Ouali.  MEAT TENDERIZATION: POSSIBLE CAUSES AND MECHANISMS. A REVIEW. , 1990 .

[16]  P. Purslow,et al.  The effect of cooking temperature on mechanical properties of whole meat, single muscle fibres and perimysial connective tissue. , 2000, Meat science.

[17]  I W Levin,et al.  Fourier transform infrared imaging: theory and practice. , 2001, Analytical chemistry.

[18]  P H Watson,et al.  Beware of connective tissue proteins: assignment and implications of collagen absorptions in infrared spectra of human tissues. , 1995, Biochimica et biophysica acta.

[19]  G. Harper.  Trends in skeletal muscle biology and the understanding of toughness in beef , 1999 .

[20]  T. Næs,et al.  Prediction of sensory characteristics of beef by near-infrared spectroscopy. , 1994, Meat science.

[21]  H. Mantsch,et al.  The use and misuse of FTIR spectroscopy in the determination of protein structure. , 1995, Critical reviews in biochemistry and molecular biology.

[22]  Y. Xiong,et al.  Thermal Denaturation of Muscle Proteins From Different Species and Muscle Types as Studied by Differential Scanning Calorimetry , 1987 .

[23]  T. Nishimura,et al.  Changes in mechanical strength of intramuscular connective tissue during postmortem aging of beef. , 1998, Journal of animal science.

[24]  V. Naik,et al.  Vibrational analysis of peptides, polypeptides, and proteins. XVII. Normal modes of crystalline Pro‐Leu‐Gly‐NH2, a type II β‐turn , 2009 .

[25]  E. Stabursvik,et al.  Myosin denaturation in pale, soft, and exudative (PSE) porcine muscle tissue as studied by differential scanning calorimetry. , 1984, Journal of the science of food and agriculture.

[26]  H. Martens,et al.  Light scattering and light absorbance separated by extended multiplicative signal correction. application to near-infrared transmission analysis of powder mixtures. , 2003, Analytical chemistry.

[27]  S. Krimm,et al.  Transition dipole coupling in Amide I modes of βpolypeptides , 1975 .

[28]  S. Engelsen,et al.  NMR-cooking: monitoring the changes in meat during cooking by low-field 1H-NMR , 2002 .

[29]  R. C. Reeder,et al.  FT-IR spectroscopic imaging microscopy of wheat kernels using a Mercury–Cadmium–Telluride focal-plane array detector , 1999 .

[30]  Peter Lasch,et al.  Characterization of Colorectal Adenocarcinoma Sections by Spatially Resolved FT-IR Microspectroscopy , 2002 .

[31]  H. Daun,et al.  Changes in texture, cooking losses, and myofibrillar structure of bovine M. semitendinosus during heating. , 1999, Meat science.