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

Journal of Agricultural and Food Chemistry

Volumn 54, Issue 18, 2006, Pages 6733-6740

  Böcker, Ulrike ^a,b   Ofstad, Ragni ^a   Bertram, Hanne Christine ^c   Egelandsdal, Bjørg ^b   Kohler, Achim ^a  

^a NORWEGIAN FOOD RESEARCH INSTITUTE   (Norway)

^b NORWEGIAN UNIVERSITY OF LIFE SCIENCES   (Norway)

^c DANISH INSTITUTE OF AGRICULTURAL SCIENCES   (Denmark)

Author keywords

Curing; FT IR microspectroscopy; Light microscopy; Pig muscle; Salting

Indexed keywords

MUSCLE PROTEIN; SODIUM CHLORIDE;

ANIMAL; ARTICLE; CHEMISTRY; DRUG EFFECT; INFRARED SPECTROSCOPY; MEAT; MUSCLE FIBRIL; PH; PROTEIN SECONDARY STRUCTURE; SKELETAL MUSCLE; SWINE; ULTRASTRUCTURE;

ANIMALS; HYDROGEN-ION CONCENTRATION; MEAT; MUSCLE PROTEINS; MUSCLE, SKELETAL; MYOFIBRILS; PROTEIN STRUCTURE, SECONDARY; SODIUM CHLORIDE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SWINE;

ANIMALIA; SUS SCROFA;

EID: 33748891216     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf060178q     Document Type: Article

References (53)

1. Arnau, J.; Guerrero, L.; Sarraga, C. The effect of green ham pH and NaCl concentration on cathepsin activities and the sensory characteristics of dry-cured hams. J. Sci. Food Agric. 1998, 77, 387-392.
2. Guerrero, L.; Gou, P.; Arnau, J. The influence of meat pH on mechanical and sensory textural properties of dry-cured ham. Meat Sci. 1999, 52, 267-273.
3. Ruiz-Ramirez, J.; Arnau, J.; Serra, X.; Gou, P. Relationship between water content, NaCl content, pH and texture parameters in dry-cured muscles. Meat Sci. 2005, 70, 579-587.
4. Garcia-Rey, R. M.; Garcia-Garrido, J. A.; Quiles-Zafra, R.; Tapiador, J.; Luque de Castro, M. D. Relationship between pH before salting and dry-cured ham quality. Meat Sci. 2004, 67, 625-632.
5. Hamm, R. Biochemistry of meat hydration. In Advances in Food Research; Chichester, C. O., Mark, E. M., Eds.; Academic Press: New York, 1960; pp 355-463.
6. Honikel, K. O. The meat aspects of water and food quality. In Water and food quality; Hardman, T. M., Ed.; Elsevier Applied Science: London, 1989.
7. Offer, G.; Trinick, J. On the mechanism of water holding in meat: The swelling and shrinking of myofibrils. Meat Sci. 1983, 8, 245-281.
8. Offer, G.; Knight, P. In Developments in meat science; Lawrie, R., Ed.; Elsevier Science Publishers Ltd.: Barking, Essex, U.K., 1988.
9. Wilding, P.; Hedges, N.; Lillford, P. J. Salt-induced swelling of meat: The effect of storage time, pH, ion-type and concentration. Meat Sci. 1986, 18, 55-75.
10. Fretheim, K.; Samejima, K.; Egelandsdal, B. Myosins from red and white bovine muscles: Part 1. Gel strength (elastisticity) and water-holding capacity of heat-induced gels. Food Chem. 1986, 22, 107-121.
11. Offer, G.; Knight, P.; Jeacocke, R.; Almond, R.; Cousins, T.; Elsey, J.; Parsons, N.; Sharp, A.; Starr, R.; Purslow, P. The structural basis of the water-holding, appearance and toughness of meat and meat-products. Food Microstruct. 1989, 8, 151-170.
12. Knight, P.; Elsey, J.; Hedges, N. The role of the endomysium in the salt-induced swelling of muscle fibres. Meat Sci. 1989, 26, 209-232.
13. Meyer, C.; Egelandsdal, B. Low deformation and water holding measurements of whole and comminuted meat originating from 2 muscles of different fibre type composition. J. Texture Stud. 1992, 23, 25-45.
14. Egelandsdal, B.; Martinsen, B. K.; Autio, K. Rheological parameters as predictors of protein functionality: A model study using myofibrils from red and white bovine muscles. Meat Sci. 1995, 39, 97-111.
15. Craig, R. W.; Padron, R. In Myology, 3rd ed.; Engel, A. G., Franzini-Armstrong, C., Eds.; McGraw-Hill: New York, 2004.
16. Kabsch, W.; Vandekerckhove, J. Structure and function of actin. Annu. Rev. Biophys. Biomol. Struct. 1992, 21, 49-76.
17. Uchida, K.; Harada, I.; Nakauchi, Y.; Maruyama, K. Structural-properties of connectin studied by ultraviolet resonance Raman-spectroscopy and infrared dichroism. FEBS Lett. 1991, 295, 35-38.
18. Kimura, S.; Matsuura, T.; Ohtsuka, S.; Nakauchi, Y.; Matsuno, A.; Maruyama, K. Characterization and localization of α-connectin (Titin-1): An elastic protein isolated from rabbit skeletal muscle. J. Muscle Res. Cell Motil. 1992, 13, 39-47.
19. Politou, A. S.; Gautel, M.; Pfuhl, M.; Labeit, S.; Pastore, A. Immunoglobulin-type domains of titin: Same fold, different stability. Biochemistry 1994, 33, 4730-4737.
20. Muhle-Goll, C.; Nilges, M.; Pastore, A. H-1 and N-15 NMR resonance assignments and secondary structure of titin type I domains. J. Biomol. NMR 1997, 9, 2-10.
21. Trinick, J.; Tskhovrebova, L. Titin: A molecular control freak. Trends Cell Biol. 1999, 9, 377-380.
22. Wright, D. J.; Wilding, P. Differential scanning calorimetric study of muscle and its proteins: Myosin and its subfragments. J. Sci. Food Agric. 1984, 35, 357-372.
23. Barbut, S.; Findlay, C. J. Influence of sodium, potassium and magnesium-chloride on thermal-properties of beef muscle. J. Food Sci. 1991, 56, 180-182.
24. Fiala, M.; Honikel, K. O. The application of the differential scanning calorimetry. Fleischwirtschaft 1995, 75, 1013-1018.
25. Diem, M.; Boydston-White, S.; Chiriboga, L. Infrared spectroscopy of cells and tissues: Shining light onto a novel subject. Appl. Spectrosc. 1999, 53, 148A-161A.
26. Diem, M.; Romeo, M.; Boydston-White, S.; Miljkovic, M.; Matthäus, C. A decade of vibrational micro-spectroscopy of human cells and tissue. Analyst 2004, 129, 880-885.
27. Fabian, H.; Mäntele, W. Infrared spectroscopy of proteins. In Handbook of Vibrational Spectroscopy; Chalmers, J. M., Griffiths, P. R., Eds.; John Wiley & Sons Ltd.: Chichester, U.K., 2002; pp 3499-3425.
28. Barth, A.; Zscherp, C. What vibrations tell us about proteins. Q. Rev. Biophys. 2002, 35, 369-430.
29. Kirschner, C.; Ofstad, R.; Skarpeid, H.-J.; Høst, V.; Kohler, A. Monitoring of denaturation processes in meat by FT-IR microspectroscopy. J. Agric. Food Chem. 2004, 52, 3920-3929.
30. Bertram, H. C.; Kohler, A.; Ofstad, R.; Böcker, U.; Andersen, H. J. 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. Agric. Food Chem. 2006, 54, 1740-1746.
31. Bertram, H. C.; Schäfer, A.; Rosenvold, K.; Andersen, H. J. Physical changes of significance for early post mortem water distribution in porcine M. longissimus. Meat Sci. 2004, 66, 915-924.
32. Henckel, P.; Karlsson, A.; Oksbjerg, N.; Petersen, J. S. Control of post mortem pH decrease in pig muscles: Experimental design and testing of animal models. Meat Sci. 2000, 55, 131-138.
33. Karlsson, A. H.; Rosenvold, K. The calibration temperature of pH-glass electrodes: Significance for meat quality classification. Meat Sci. 2002, 62, 497-501.
34. Lillie, R. D.; Fullmer, H. M. Histopathologic technic and practical histochemistry; McGraw-Hill: New York, 1976.
35. Engdahl, A.; Kolar, K. Metodeforskrift 22.6.93 Koksaltbestämning med Corning 926 Chloride Analyzer, Köttforskningsinstitut i Kävlinge, 1993.
36. Nordisk Metodikkommite for næringsmidler, NMKL-metode nr 23, 1991.
37. Martens, H.; Stark, E. Extended multiplicative signal correction and spectral interference subtraction: New preprocessing methods for near-infrared spectroscopy. J. Pharm. Biomed. Anal. 1991, 9, 625-635.
38. Kohler, A.; Kirschner, C.; Oust, A.; Martens, H. Extended multiplicative signal correction as a tool for separation and characterization of physical and chemical information in Fourier transform infrared microscopy images of cryo-sections of beef loin. Appl. Spectrosc. 2005, 59, 707-716.
39. DeNoyer, L. K.; Dodd, J. G. Smoothing and derivatives in spectroscopy. In Handbook of Vibrational Spectroscopy, Chalmers, J. M., Griffiths, P. R., Eds.; John Wiley & Sons Ltd.: Chichester, U.K., 2002; pp 2173-2183.
40. Martens, H.; Martens, M. Multivariate Analysis of Quality: An Introduction; John Wiley & Sons, Ltd.: Chichester, U.K., 2001.
41. Wold, S.; Martens, H.; Wold, H. The multivariate calibration problem in chemistry solved by the PLS method. In Proceedings of the Conference on Matrix Pencils; Springer-Verlag, Heidelberg, Germany, 1983; pp 286-293.
42. Jackson, M.; Mantsch, H. H. The use and misuse of FTIR spectroscopy in the determination of protein-structure. Crit. Rev. Biochem. Mol. Biol. 1995, 30, 95-120.
43. Jackson, M.; Choo, L. P.; Watson, P. H.; Halliday, W. C.; Mantsch, H. H. Beware of connective-tissue proteins: Assignment and implications of collagen absorptions in infrared-spectra of human tissues. Biochim. Biophys. Acta 1995, 1270, 1-6.
44. Sokrates, G. Infrared and Roman Characteristic Group Frequencies. Tables and Charts, 3rd ed.; John Wiley & Sons Ltd.: Chichesler, U.K., 2001.
45. Chu, H. L.; Liu, T. Y.; Lin, S. Y. Effect of cyanide concentrations on the secondary structures of protein in the crude homogenates of the fish gill tissue. Aquat. Toxicol. 2001, 55, 171-176.
46. Greaser, M. L. Conversion of muscle to meat. In Muscle as food; Bechtel, P. J., Ed.; Academic Press: London, 1986; pp 37-102.
47. Thorarinsdottir, K. A.; Arason, S.; Bogason, S. G.; Kristbergsson, K. The effects of various sail concentrations during brine curing of cod (Gadus morhua). Int. J. Food Sci. Technol. 2004, 39, 79-89.
48. Lawrie, R. A. Lawrie's Meat Science, 6th ed.; Woodhead Publishing Ltd.: Cambridge, U.K., 1998.
49. Rao, M. V.; Gault, N. F. S. The influence of fibre-type composition and associated biochemical characteristics on the acid buffering capacities of several beef muscles. Meat Sci. 1989, 26, 5-18.
50. Ofstad, R.; Kidman, S.; Myklebust, R.; Olsen, R. L.; Hermansson, A. M. Liquid-holding capacity and structural-changes in comminuted salmon (Salmo-Salar) muscle as influenced by pH, salt and temperature. Food Sci. Technol. 1995, 28, 329-339.
51. Irving, T. C.; Swatland, H. J.; Millman, B. M. Effect of pH on myofilament spacing in pork measured by X-ray-diffraction. Can. Inst. Food Sci. Technol. J. 1990, 23, 79-81.
52. Guignot, F.; Vignon, X.; Monin, G. Postmortem evolution of myofilament spacing and extracellular-space in veal muscle. Meat Sci. 1993, 33, 333-347.
53. Stafford, W. F. Effect of various anions on the stability of the coiled coil of skeletal-muscle myosin. Biochemistry 1985, 24, 3314-3321.