Hyperspectral deep ultraviolet autofluorescence of muscle fibers is affected by postmortem changes.

After slaughter, muscle cells undergo biochemical and physicochemical changes that may affect their autofluorescence characteristics. The autofluorescent response of different rat extensor digitorum longus (EDL) and soleus muscle fiber types was investigated by deep ultraviolet (UV) synchrotron microspectroscopy immediately after animal sacrifice and after 24 h of storage in a moist chamber at 20 °C. The glycogen content decreased from 23 to 18 μmol/g of fresh muscle in 24 h postmortem. Following a 275 nm excitation wavelength, the spectral muscle fiber autofluorescence response showed discrimination depending upon postmortem time (t0 versus t24 h) on both muscles at 346 and 302 nm and, to a lesser extent, at 408 and 325 nm. Taken individually, all fiber types were discriminated but with variable accuracy, with type IIA showing better separation of t0/t24 h than other fiber types. These results suggest the usefulness of the autofluorescent response of muscle cells for rapid meat-aging characterization.

[1]  M. Desvaux,et al.  Deep UV excited muscle cell autofluorescence varies with the fibre type. , 2015, The Analyst.

[2]  M. Réfrégiers,et al.  Protein matrix involved in the lipid retention of foie gras during cooking: a multimodal hyperspectral imaging study. , 2014, Journal of agricultural and food chemistry.

[3]  S. Lauzurica,et al.  Effect of lairage time ( 0h, 3 h, 6 h or 12 h) on glycogen content and meat quality parameters in suckling lambs. , 2014, Meat science.

[4]  T. Astruc Muscle Structure and Digestive Enzyme Bioaccessibility to Intracellular Compartments , 2014 .

[5]  T. Astruc,et al.  MUSCLE FIBER TYPES AND MEAT QUALITY , 2014 .

[6]  Frédéric Jamme,et al.  Deep UV autofluorescence microscopy for cell biology and tissue histology , 2013, Biology of the cell.

[7]  N. Fujii,et al.  Exercise training‐induced adaptations associated with increases in skeletal muscle glycogen content , 2013, The FEBS journal.

[8]  C. Benhamou,et al.  Synchrotron Ultraviolet Microspectroscopy on Rat Cortical Bone: Involvement of Tyrosine and Tryptophan in the Osteocyte and Its Environment , 2012, PloS one.

[9]  J. Quadrilatero,et al.  Rapid Determination of Myosin Heavy Chain Expression in Rat, Mouse, and Human Skeletal Muscle Using Multicolor Immunofluorescence Analysis , 2012, PloS one.

[10]  Frank Wien,et al.  Synchrotron UV Fluorescence Microscopy Uncovers New Probes in Cells and Tissues , 2010, Microscopy and Microanalysis.

[11]  M. Réfrégiers,et al.  Multimodal spectroscopy combining time-of-flight-secondary ion mass spectrometry, synchrotron-FT-IR, and synchrotron-UV microspectroscopies on the same tissue section. , 2010, Analytical chemistry.

[12]  L. Lefaucheur A second look into fibre typing--relation to meat quality. , 2010, Meat science.

[13]  Daniel Zerbib,et al.  DISCO: a low-energy multipurpose beamline at synchrotron SOLEIL. , 2009, Journal of synchrotron radiation.

[14]  Avraham Mayevsky,et al.  Mitochondrial function in vivo evaluated by NADH fluorescence: from animal models to human studies. , 2007 .

[15]  K. Punkt,et al.  Differentiation of rat skeletal muscle fibres during development and ageing. , 2004, Acta histochemica.

[16]  P. Berge,et al.  Development of Intrinsic Fluorescent Multispectral Imagery Specific for Fat, Connective Tissue, and Myofibers in Meat , 2003 .

[17]  E. Dufour,et al.  Measure of meat tenderness using front-face fluorescence spectroscopy , 2003 .

[18]  Eric Dufour,et al.  Development of a rapid method based on front-face fluorescence spectroscopy for the monitoring of fish freshness , 2003 .

[19]  E. Neyraud,et al.  Effects of halothane genotype and pre-slaughter treatment on pig meat quality. Part 1. Post mortem metabolism, meat quality indicators and sensory traits of m. Longissimus lumborum. , 2002, Meat science.

[20]  C. Berri,et al.  Effects of the rate of muscle post mortem pH fall on the technological quality of turkey meat , 2002, British poultry science.

[21]  T. Astruc,et al.  Temperature and catecholamine effects on metabolism of perfused isolated rabbit muscle. , 2002, Meat science.

[22]  C. Berri,et al.  Post mortem muscle metabolism and meat quality in three genetic types of turkey , 2001, British poultry science.

[23]  M. Ruusunen,et al.  Bovine muscle glycogen concentration in relation to finishing diet, slaughter and ultimate pH. , 2000, Meat science.

[24]  G. Monin,et al.  Muscle glycogen level and meat quality in pigs of different halothane genotypes. , 1995, Meat science.

[25]  M. Koohmaraie,et al.  Muscle proteinases and meat aging. , 1994, Meat science.

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

[27]  P. Calder,et al.  Post mortem glycogenolysis is a combination of phosphorolysis and hydrolysis. , 1990, The International journal of biochemistry.

[28]  J. Henriksson,et al.  NADH content in type I and type II human muscle fibres after dynamic exercise. , 1988, The Biochemical journal.

[29]  J. Lakowicz Principles of fluorescence spectroscopy , 1983 .

[30]  P. V. Tarrant,et al.  Glycogen content and repletion rates in beef muscle, effect of feeding and fasting. , 1982, The Journal of nutrition.

[31]  T. R. Dutson,et al.  ULTRASTRUCTURAL POSTMORTEM CHANGES IN NORMAL AND LOW QUALITY PORCINE MUSCLE FIBERS , 1974 .

[32]  J. R. Bendall 5 – POSTMORTEM CHANGES IN MUSCLE , 1973 .