Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes.

Unacceptable water-holding capacity costs the meat industry millions of dollars annually. However, limited progress has been made toward understanding the mechanisms that underlie the development of drip or purge. It is clear that early postmortem events including rate and extent of pH decline, proteolysis and even protein oxidation are key in influencing the ability of meat to retain moisture. Much of the water in the muscle is entrapped in structures of the cell, including the intra- and extramyofibrillar spaces; therefore, key changes in the intracellular architecture of the cell influence the ability of muscle cells to retain water. As rigor progresses, the space for water to be held in the myofibrils is reduced and fluid can be forced into the extramyofibrillar spaces where it is more easily lost as drip. Lateral shrinkage of the myofibrils occurring during rigor can be transmitted to the entire cell if proteins that link myofibrils together and myofibrils to the cell membrane (such as desmin) are not degraded. Limited degradation of cytoskeletal proteins may result in increased shrinking of the overall muscle cell, which is ultimately translated into drip loss. Recent evidence suggests that degradation of key cytoskeletal proteins by calpain proteinases has a role to play in determining water-holding capacity. This review will focus on key events in muscle that influence structural changes that are associated with water-holding capacity.

[1]  C. Thornton,et al.  Identification of a Novel AMP-activated Protein Kinase β Subunit Isoform That Is Highly Expressed in Skeletal Muscle* , 1998, The Journal of Biological Chemistry.

[2]  Hanne Christine Bertram,et al.  Relationship between meat structure, water mobility, and distribution: a low-field nuclear magnetic resonance study. , 2002, Journal of agricultural and food chemistry.

[3]  H J Swatland,et al.  A review of the relationships of pH with physical aspects of pork quality. , 1988, Meat science.

[4]  J. Dekkers,et al.  New alleles in calpastatin gene are associated with meat quality traits in pigs. , 2004, Journal of animal science.

[5]  Ralston Lawrie,et al.  Developments in meat science , 1980 .

[6]  B. Essén-Gustavsson,et al.  Effect of halothane genotype on muscle metabolism at slaughter and its relationship with meat quality: A within-litter comparison. , 1989, Meat science.

[7]  P. Purslow,et al.  The effect of ageing on the water-holding capacity of pork: role of cytoskeletal proteins. , 2001, Meat science.

[8]  E. Huff-Lonergan,et al.  Proteolysis of specific muscle structural proteins by mu-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. , 1996, Journal of animal science.

[9]  M. Greaser An Overview of the Muscle Cell Cytoskeleton , 2001 .

[10]  G. Geesink,et al.  Postmortem proteolysis and calpain/calpastatin activity in callipyge and normal lamb biceps femoris during extended postmortem storage. , 1999, Journal of animal science.

[11]  E. Huff-Lonergan,et al.  Early postmortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles. , 2004, Journal of animal science.

[12]  J. Trinick,et al.  On the mechanism of water holding in meat: The swelling and shrinking of myofibrils. , 1983, Meat science.

[13]  M. Carlson,et al.  The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell? , 1998, Annual review of biochemistry.

[14]  E. Huff-Lonergan,et al.  Oxidative environments decrease tenderization of beef steaks through inactivation of mu-calpain. , 2004, Journal of animal science.

[15]  G. Offer,et al.  Modelling of the formation of pale, soft and exudative meat: Effects of chilling regime and rate and extent of glycolysis. , 1991, Meat science.

[16]  E. Huff-Lonergan,et al.  Effect of pH and ionic strength on mu- and m-calpain inhibition by calpastatin. , 2005, Journal of animal science.

[17]  H. J. Andersen,et al.  Factors of significance for pork quality-a review. , 2003, Meat science.

[18]  R. Hamm 16 – WATER-HOLDING CAPACITY OF MEAT , 1975 .

[19]  H. J. Andersen,et al.  Physiological and structural events post mortem of importance for drip loss in pork. , 2002, Meat science.

[20]  H. Lee,et al.  Interaction of talin with actin: sensitive modulation of filament crosslinking activity. , 1999, Archives of biochemistry and biophysics.

[21]  Alan K. Soper,et al.  Water and Ice , 2002, Science.

[22]  B. Millman,et al.  Lateral forces in the filament lattice of vertebrate striated muscle in the rigor state. , 1983, Biophysical journal.

[23]  D. E. Goll,et al.  The calpain system. , 2003, Physiological reviews.

[24]  B. Millman,et al.  X-ray diffraction measurements of postmortem changes in the myofilament lattice of pork. , 1988, Journal of animal science.

[25]  P. Bechtel Muscle as food , 1986 .

[26]  S. W. Sernett,et al.  Properties of the novel intermediate filament protein synemin and its identification in mammalian muscle. , 1998, Archives of biochemistry and biophysics.

[27]  K. Wang,et al.  A network of transverse and longitudinal intermediate filaments is associated with sarcomeres of adult vertebrate skeletal muscle , 1983, The Journal of cell biology.

[28]  P. D. Bell,et al.  ‘Oxidation Inhibits Substrate Proteolysis by Calpain I but Not Autolysis* , 1997, The Journal of Biological Chemistry.

[29]  E. Stadtman,et al.  Carbonyl assays for determination of oxidatively modified proteins. , 1994, Methods in enzymology.

[30]  R. Winger,et al.  Osmotic properties of post-rigor beef muscle. , 1981, Meat science.

[31]  T. R. Dutson,et al.  Effect of Low‐Calcium‐Requiring Calcium Activated Factor on Myofibrils under Varying pH and Temperature Conditions , 1986 .

[32]  S. Williams,et al.  Effect of pH and ionic strength on bovine m-calpain and calpastatin activity. , 1993, Journal of animal science.

[33]  P. Hegarty Differences in fibre size of histologically processed pre- and post-rigor mouse skeletal muscle. , 1970, Life sciences. Pt. 2: Biochemistry, general and molecular biology.

[34]  R. Johnson,et al.  Correlated response in placental efficiency in swine selected for an index of components of lifter size. , 2003, Journal of animal science.

[35]  E. Huff-Lonergan,et al.  Influence of early postmortem protein oxidation on beef quality. , 2004, Journal of animal science.

[36]  Allen J. Bailey,et al.  Connective Tissue in Meat and Meat Products , 1989 .

[37]  M. Rothschild,et al.  Evidence for new alleles in the protein kinase adenosine monophosphate-activated gamma(3)-subunit gene associated with low glycogen content in pig skeletal muscle and improved meat quality. , 2001, Genetics.

[38]  H. Thier Principles of Food Science. Part 1: Food Chemistry. Herausgegeben von O. R. Fennema. Marcel Dekker Inc., New York‐Basel 1976. 1. Aufl., XI, 792 S., geb. sfr. 170.— , 1976 .

[39]  R. Robson,et al.  Purified desmin from adult mammalian skeletal muscle: a peptide mapping comparison with desmins from adult mammalian and avian smooth muscle. , 1979, Biochemical and biophysical research communications.

[40]  P. Purslow,et al.  Immunolocalisation of intermediate filament proteins in porcine meat. Fibre type and muscle-specific variations during conditioning. , 1998, Meat science.

[41]  C. Rogel-Gaillard,et al.  A mutation in PRKAG3 associated with excess glycogen content in pig skeletal muscle. , 2000, Science.

[42]  M. Dikeman,et al.  Evaluation of attributes that affect longissimus muscle tenderness in Bos taurus and Bos indicus cattle. , 1990, Journal of animal science.

[43]  L. Skibsted,et al.  Effect of pre-slaughter physiological conditions on the oxidative stability of colour and lipid during chill storage of pork. , 2001, Meat science.

[44]  E. Stadtman,et al.  Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences. , 1990, Free radical biology & medicine.

[45]  M. Koohmaraie,et al.  Effect of pH, temperature, and inhibitors on autolysis and catalytic activity of bovine skeletal muscle mu-calpain. , 1992, Journal of animal science.

[46]  P. Gatellier,et al.  Comparison of Oxidative Processes on Myofibrillar Proteins from Beef during Maturation and by Different Model Oxidation Systems , 1997 .

[47]  The AMP‐Activated Protein Kinase , 1997 .

[48]  P. Purslow,et al.  The Structural Basis of the Water-Holding, Appearance and Toughness of Meat and Meat Products , 1989 .

[49]  D. Carling,et al.  Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding. , 2000, The Biochemical journal.

[50]  B. Millman,et al.  Effects of hyperosmotic solutions on the filament lattice of intact frog skeletal muscle. , 1981, Biophysical journal.

[51]  G. Önning,et al.  Glutathione peroxidase activity, tissue and soluble selenium content in beef and pork in relation to meat ageing and pig RN phenotype , 2001 .

[52]  G. Offer,et al.  The mechanism of drip production: Formation of two compartments of extracellular space in muscle Post mortem , 1992 .

[53]  P. D. Jolley,et al.  The amount and composition of the proteins in drip from stored pig meat. , 1990, Meat science.

[54]  Kathy J. Davis,et al.  The effects of aging on moisture-enhanced pork loins. , 2004, Meat science.

[55]  E. Huff-Lonergan,et al.  POSTMORTEM PROTEOLYSIS AND TENDERIZATION OF TOP LOIN STEAKS FROM BRANGUS CATTLE , 2001 .

[56]  H. Haagsman,et al.  Muscle Development of Livestock Animals: Physiology, Genetics and Meat Quality , 2004 .

[57]  R. Robson,et al.  Properties of smooth muscle vinculin. , 1984, The Journal of biological chemistry.

[58]  T. Koh,et al.  Nitric oxide inhibits calpain-mediated proteolysis of talin in skeletal muscle cells. , 2000, American journal of physiology. Cell physiology.

[59]  K. Wang,et al.  Casein zymography: a method to study mu-calpain, m-calpain, and their inhibitory agents. , 1995, Archives of biochemistry and biophysics.

[60]  G. Johnson,et al.  Oxidative Stress Inhibits Calpain Activity in Situ * , 1998, The Journal of Biological Chemistry.

[61]  S. E. Harris,et al.  Antioxidant status affects color stability and tenderness of calcium chloride-injected beef. , 2001, Journal of animal science.

[62]  K. Otsu,et al.  Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia. , 1991, Science.

[63]  E. Decker,et al.  ALTERATIONS OF MUSCLE PROTEIN FUNCTIONALITY BY OXIDATIVE AND ANTIOXIDATIVE PROCESSES , 1995 .

[64]  R. Hamm Functional Properties of the Myofibrillar System and Their Measurements , 1986 .

[65]  D. Hardie,et al.  The AMP-activated protein kinase--fuel gauge of the mammalian cell? , 1997, European journal of biochemistry.

[66]  G. Monin,et al.  Pork of low technological quality with a normal rate of muscle pH fall in the immediate post-mortem period: The case of the Hampshire breed. , 1985, Meat science.

[67]  K. Honikel,et al.  Sarcomere shortening of prerigor muscles and its influence on drip loss. , 1986, Meat science.

[68]  H. Swatland,et al.  Post mortem changes in the shape and size of myofibrils from skeletal muscle of pigs , 1985 .

[69]  F. Shahidi,et al.  Quality attributes of muscle foods , 1999 .

[70]  J. R. Bendall,et al.  Some Properties of the Fibrillar Proteins of Normal and Watery Pork Muscle , 1962 .