Role of calpain system in meat tenderness: A review

Food Science and Human Wellness - Tập 7 - Trang 196-204 - 2018
Z.F. Bhat1, James D. Morton1, Susan L. Mason1, Alaa El-Din A. Bekhit2
1Department of Wine Food and Molecular Biosciences, Faculty of Agriculture and Life Sciences, Lincoln University, Lincoln, 7647, Christchurch, New Zealand
2Department of Food Sciences, University of Otago, P.O. Box 56, Dunedin, 9054, New Zealand

Tài liệu tham khảo

Hopkins, 2009, 149 Sierra, 2013, Role of mitochondria on muscle cell death and meat tenderization, Recent Pat. Endocr. Metab. Immune Drug Discov., 7, 120, 10.2174/1872214811307020005 Taylor, 1995, Is Z-disk degradation responsible for postmortem tenderization?, J. Anim. Sci., 73, 1351, 10.2527/1995.7351351x Wheeler, 1994, Prerigor and postrigor changes in tenderness of ovine longissimus muscle, J. Anim. Sci., 72, 1232, 10.2527/1994.7251232x Geesink, 1999, Effect of calpastatin on degradation of myofibrillar proteins by l-calpain under postmortem conditions, J. Anim. Sci., 77, 2685, 10.2527/1999.77102685x Bekhit, 2007, Effects of rigor temperature and electrical stimulation on venison quality, Meat Sci., 75, 564, 10.1016/j.meatsci.2006.09.005 Geesink, 2000, Rigor temperature and meat quality characteristics of lamb longissimus muscle, J. Anim. Sci., 78, 2842, 10.2527/2000.78112842x Hertzman, 1993, The influence of high temperature, type of muscle and electrical stimulation on the course of rigor, aging and tenderness of beef muscles, Meat Sci., 35, 119, 10.1016/0309-1740(93)90074-R Warner, 2014, Factors influencing the incidence of high rigor temperature in beef carcasses in Australia, Anim. Prod. Sci., 54, 363, 10.1071/AN13455 Thompson, 2005, The impact of processing on sensory and objective measurements of sheep meat eating quality, Aust. J. Exp. Agric., 45, 561, 10.1071/EA03195 Lonergan, 2010, Biochemistry of postmortem muscle-Lessons on mechanisms of meat tenderization, Meat Sci., 86, 184, 10.1016/j.meatsci.2010.05.004 Savell, 2005, The chilling of carcasses. Review, Meat Sci., 70, 449, 10.1016/j.meatsci.2004.06.027 Fernández, 2012, Effect of chilling applied to suckling lamb carcasses on hygienic, physicochemical and sensory meat quality, Meat Sci., 92, 569, 10.1016/j.meatsci.2012.05.029 Vieira, 2014, Effect of aging time on suckling lamb meat quality resulting from different carcass chilling regimes, Meat Sci., 96, 682, 10.1016/j.meatsci.2013.09.017 Rees, 2002, Tenderness, aging rate and meat quality of pork M. longissimus thoracis et lumborum after accelerated boning, Meat Sci., 60, 113, 10.1016/S0309-1740(01)00085-7 Marsh, 1954, Rigor mortis in beef, J. Sci. Food Agric., 5, 70, 10.1002/jsfa.2740050202 Rosenvold, 2010, Stepwise chilling- Tender pork without compromising water-holding capacity, J. Anim. Sci., 88, 1830, 10.2527/jas.2009-2468 Rees, 2003, The influence of the rate of pH decline on the rate of aging for pork. II: interaction with chilling temperature, Meat Sci., 65, 805, 10.1016/S0309-1740(02)00285-1 Leroy, 2003, Prediction of technological and organoleptic properties of beef Longissimus thoracis from near-infrared reflectance and transmission spectra, Meat Sci., 66, 45, 10.1016/S0309-1740(03)00002-0 Khan, 2016, Postmortem aging of beef with a special reference to the dry aging, Korean J. Food Anim. Sci., 36, 159, 10.5851/kosfa.2016.36.2.159 Smith, 2007 Campbell, 2001, Dry-aging effects on palatability of beef longissimus muscle, J. Food Sci., 66, 196, 10.1111/j.1365-2621.2001.tb11315.x Bowling, 1987, Effect of cryogenic chilling on beef carcass grade, shrinkage and palatability characteristics, Meat Sci., 21, 67, 10.1016/0309-1740(87)90042-8 Joseph, 1996, Very fast chilling of beef and tenderness- A report from an EU concerted action, Meat Sci., 43, 217, 10.1016/0309-1740(96)00067-8 Hwang, 2003, The biochemical and physical effects of electrical stimulation on beef and sheep meat tenderness, Meat Sci., 65, 677, 10.1016/S0309-1740(02)00271-1 Miller, 1985, Effect of subprimal fabrication and packaging methods on palatability and retail caselife of loin steaks from lean beef, J. Food Sci., 50, 1544, 10.1111/j.1365-2621.1985.tb10529.x Melody, 2004, Early postmortem biochemical factors influence tenderness and water holding capacity of three porcine muscles, J. Anim. Sci., 82, 1195, 10.2527/2004.8241195x Lochner, 1980, Early-postmortem cooling rate and beef tenderness, Meat Sci., 4, 227, 10.1016/0309-1740(80)90051-0 Simmons, 2008, Reassessing the principles of electrical stimulation, Meat Sci., 80, 110, 10.1016/j.meatsci.2008.05.006 Carlin, 2006, Effect of oxidation, pH, and ionic strength on calpastatin inhibition of mu- and m-calpain, J. Anim. Sci., 84, 925, 10.2527/2006.844925x Totland, 1988, Composition of muscle fibre types and connective tissue in bovine M. semitendinosus and its relation to tenderness, Meat Sci., 23, 303, 10.1016/0309-1740(88)90014-9 Ouali, 1990, Calpains and calpastatin distribution in bovine, porcine and ovine skeletal-muscles, Meat Sci., 28, 331, 10.1016/0309-1740(90)90047-A Koohmaraie, 1996, Biochemical factors regulating the toughening and tenderisation process of meat, Meat Sci., 43, 193, 10.1016/0309-1740(96)00065-4 Xiong, 2004, Protein functionality, 218 Seideman, 1986, The effect of sex condition and growth implants on bovine muscle fiber characteristics, Meat Sci., 17, 79, 10.1016/0309-1740(86)90056-2 Choi, 2007, Influence of myosin heavy- and light chain isoforms on early postmortem glycolytic rate and pork quality, Meat Sci., 76, 281, 10.1016/j.meatsci.2006.11.009 Joo, 2013, Control of fresh meat quality through manipulation of muscle fiber characteristics, Meat Sci., 95, 828, 10.1016/j.meatsci.2013.04.044 Hwang, 2010, The relationship between muscle fiber characteristics and meat quality traits of highly marbled Hanwoo (Korean native cattle) steers, Meat Sci., 86, 456, 10.1016/j.meatsci.2010.05.034 Ozawa, 2000, The characteristics of muscle fiber types of longissimus thoracis muscle and their influences on the quantity and quality of meat from Japanese Black steers, Meat Sci., 54, 65, 10.1016/S0309-1740(99)00072-8 Kirchofer, 2002, Fiber type composition of muscles of the beef chuck and round, J. Anim. Sci., 80, 2872, 10.2527/2002.80112872x Rhee, 2004, Variation in palatability and biochemical traits within and among eleven beef muscles, J. Anim. Sci., 82, 534, 10.2527/2004.822534x Hopkins, 2001, The relationship between tenderness, proteolysis, muscle contraction and dissociation of actomyosin, Meat Sci., 57, 1, 10.1016/S0309-1740(00)00065-6 Redmond, 2001, The effect of ultra-rapid chilling and subsequent aging on the calpain/calpastatin system and myofibrillar degradation in lambM. longissimus thoracis et lumborum, Meat Sci., 59, 293, 10.1016/S0309-1740(01)00082-1 Wheeler, 1999, The extent of proteolysis is independent of sarcomere length in lamb longissimus and psoas major, J. Anim. Sci., 77, 2444, 10.2527/1999.7792444x Weaver, 2009, Sarcomere length influences calpain mediated proteolysis of bovine myofibrils, J. Anim. Sci., 87, 2096, 10.2527/jas.2008-1317 Sorheim, 2002, Muscle stretching techniques for improving meat tenderness, Trends Food Sci. Technol., 13, 127, 10.1016/S0924-2244(02)00069-9 Dransfield, 1994, Optimization of tenderization, aging and tenderness, Meat Sci., 36, 105, 10.1016/0309-1740(94)90037-X Jaime, 1993, Tenderization of lamb meat: effect of rapid temperature drop on muscle conditioning and aging, Meat Sci., 32, 357, 10.1016/0309-1740(92)90078-I Hughes, 2014, A structural approach to understanding the interactions between colour, water-holding capacity and tenderness, Meat Sci., 98, 520, 10.1016/j.meatsci.2014.05.022 Huff-Lonergan, 1996, Proteolysis of specific muscle structural proteins by mucalpain at low pH and temperature is similar to degradation in post-mortem bovine muscle, J. Anim. Sci., 74, 993, 10.2527/1996.745993x Hopkins, 2002, The degradation of myofibrillar proteins in beef and lamb using denaturing electrophoresis–An overview, J. Muscle Foods., 13, 81, 10.1111/j.1745-4573.2002.tb00323.x Ouali, 2006, Revisiting the conversion of muscle into meat and the underlying mechanisms, Meat Sci., 74, 44, 10.1016/j.meatsci.2006.05.010 Geesink, 2006, μ-Calpain is essential for postmortem proteolysis of muscle proteins, J. Anim. Sci., 84, 2834, 10.2527/jas.2006-122 Koohmaraie, 2006, Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system, Meat Sci., 74, 34, 10.1016/j.meatsci.2006.04.025 Huff-Lonergan, 1999, Postmortem mechanisms of meat tenderization: the roles of the structural proteins and the calpain system, 229 Koohmaraie, 1992, The role of Ca2+-dependent proteases (calpains) in postmortem proteolysis and meat tenderness, Biochimie, 74, 239, 10.1016/0300-9084(92)90122-U Koohmaraie, 1991, Postmortem proteolysis in longissimus muscle from beef, lamb and pork carcasses, J. Anim. Sci., 69, 617, 10.2527/1991.692617x Kendall, 1993, Effect of pH and ionic strength on bovine m-calpain and calpastatin activity, J. Anim. Sci., 71, 96, 10.2527/1993.71196x Dayton, 1976, A Ca2+-activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme, Biochemistry, 15, 2159, 10.1021/bi00655a020 Kent, 2004, Postmortem proteolysis is reduced in transgenic mice overexpressing calpastatin, J. Anim. Sci., 82, 794, 10.2527/2004.823794x Bohorov, 1987, The effect of the β-2-adrenergic agonist clenbuterol or implantation with oestradiol plus trenbolone acetate on protein metabolism in wether lambs, British J. Nutr., 57, 99, 10.1079/BJN19870013 Dunshea, 2005, Effects of dietary factors and other metabolic modifiers on quality and nutritional value of meat, Meat Sci., 71, 8, 10.1016/j.meatsci.2005.05.001 Geesink, 1999, Postmortem proteolysis and calpain/calpastatin activity in callipyge and normal lamb biceps femoris during extended postmortem storage, J. Anim. Sci., 77, 1490, 10.2527/1999.7761490x Wheeler, 1997, Effect of postmortem injection time and postinjection aging time on the calcium-activated tenderization process in beef, J. Anim. Sci., 75, 2652, 10.2527/1997.75102652x Koohmaraie, 1989, Acceleration of post-mortem tenderization in ovine carcasses through infusion of calcium chloride: Effect of concentration and ionic strength, J. Anim. Sci., 67, 934, 10.2527/jas1989.674934x Sentandreu, 2002, Role of muscle endopeptidases and their inhibitors in meat tenderness, Trends Food Sci. Technol., 13, 400, 10.1016/S0924-2244(02)00188-7 Croall, 1991, Calcium-activated neutral protease (calpain) system: Structure, function, and regulation, Physiol. Rev., 71, 813, 10.1152/physrev.1991.71.3.813 Goll, 2003, The calpain system, Physiol. Rev., 83, 731, 10.1152/physrev.00029.2002 Cruzen, 2013 Moudilou, 2010, Calpains expression during Xenopus Laevis development, Tissue Cell, 42, 275, 10.1016/j.tice.2010.07.001 Ilian, 2004, Postmortem changes in myofibrillar-bound calpain 3 revealed by immunofluorescence microscopy, Meat Sci., 66, 231, 10.1016/S0309-1740(03)00096-2 Xu, 2009, Development and application of a real-time PCR method for pharmacokinetic and biodistribution studies of recombinant adenovirus, Mol. Biotechnol., 43, 130, 10.1007/s12033-009-9173-9 Tullio, 1999, Changes in intracellular localization of calpastatin during calpain activation, Biochem., 343, 467, 10.1042/bj3430467 Suzuki, 1990, The structure of calpains and the calpain gene, 25 Toldra, 2015, Enzymes in meat and fish, 199 Nishimura, 1991, Binding of calpain fragments to calpastatin, J. Biol. Chem., 266, 11842, 10.1016/S0021-9258(18)99034-4 Strobl, 2000, The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium, Proc. Natl. Acad. Sci., 97, 588, 10.1073/pnas.97.2.588 Tompa, 2001, Domain III of calpain is a Ca2+-regulated phospholipid-binding domain, Biochem. Biophys. Res. Commun., 280, 1333, 10.1006/bbrc.2001.4279 Suzuki, 2004, Structure, activation, and biology of calpain, Diabetes., 53, S12, 10.2337/diabetes.53.2007.S12 Campbell, 2012, Structure–function relationships in calpains, Biochem., 447, 335, 10.1042/BJ20120921 Raynaud, 2005, Correlation between bovine calpastatin mRNA transcripts and protein isoforms, Arch. Biochem. Biophys., 440, 46, 10.1016/j.abb.2005.05.028 Wendt, 2004, Interaction of calpastatin with calpain: A review, J. Biol. Chem., 385, 465 Sorimachi, 1989, Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle, J. Biol. Chem., 264, 20106, 10.1016/S0021-9258(19)47225-6 Ravulapalli, 2005, Homodimerization of calpain 3 penta-EF-hand domain, Biochem., 388, 585, 10.1042/BJ20041821 Hanna, 2008, Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin, Nature., 456, 409, 10.1038/nature07451 Elce, 1997, The effects of truncations of the small subunit on m-calpain activity and heterodimer formation, Biochem., 326, 31, 10.1042/bj3260031 Hosfield, 1999, Crystal structure of calpain reveals the structural basis for Ca2+-dependent protease activity and a novel mode of enzyme activation, EMBO J., 18, 6880, 10.1093/emboj/18.24.6880 Moldoveanu, 2002, A Ca2+ switch aligns the active site of calpain, Cell., 108, 649, 10.1016/S0092-8674(02)00659-1 Benyamin, 2006, The structural basis of calpain behaviour, FEBS J., 273, 3413, 10.1111/j.1742-4658.2006.05353.x Salamino, 1993, Site-directed activation of calpain is promoted by a membrane-associated natural activator protein, Biochem., 290, 191, 10.1042/bj2900191 Saido, 1992, Positive regulation of mu-calpain action by polyphosphoinositides, J. Biol. Chem., 267, 24585, 10.1016/S0021-9258(18)35804-6 Fan, 2013, LabCaS: Labeling calpain substrate cleavage sites from amino acid sequence using conditional random fields, Proteins: Struct. Funct. Bioinf., 81, 622, 10.1002/prot.24217 duVerle, 2011, Calpain cleavage prediction using multiple kernel learning, PLoS ONE, 6, 10.1371/journal.pone.0019035 Sorimachi, 2012, Understanding the substrate specificity of conventional calpains, Biol. Chem., 393, 853, 10.1515/hsz-2012-0143 Kawasaki, 1996, Regulation of the calpain calpastatin system by membranes, Mol. Membr. Biol., 13, 217, 10.3109/09687689609160599 Tullio, 2007, Multiple rat brain calpastatin forms are produced by distinct starting points and alternative splicing of the N-terminal exons, Arch. Biochem. Biophy., 465, 148, 10.1016/j.abb.2007.05.007 Mohrhauser, 2011, In vitro degradation of bovine myofibrils is caused by μ-calpain, not caspase-3, J. Anim. Sci., 89, 798, 10.2527/jas.2010-3149 Ji, 2006, Changes in concentration of sarcoplasmic free calcium during post-mortem aging of meat, Meat Sci., 73, 395, 10.1016/j.meatsci.2005.09.010 Koohmaraie, 1988, Acceleration of postmortem tenderization in ovine carcasses through activation of Ca2+-dependent proteases, J. Food Sci., 53, 1638, 10.1111/j.1365-2621.1988.tb07803.x Koohmaraie, 1987, Effect of post-mortem storage on Ca++-dependent proteases, their inhibitor and myofibril fragmentation, Meat Sci., 19, 187, 10.1016/0309-1740(87)90056-8 Sensky, 1996, The relationship between plasma epinephrine concentration and the activity of the calpain enzyme system in porcine longissimus muscle, J. Anim. Sci., 74, 380, 10.2527/1996.742380x Camou, 2007, Effect of postmortem storage on activity of μ- and m-calpain in five bovine muscles, J. Anim. Sci., 85, 2670, 10.2527/jas.2007-0164 Zhang, 2006, Contribution of postmortem changes of integrin, desmin and mu-calpain to variation in water holding capacity of pork, Meat Sci., 74, 578, 10.1016/j.meatsci.2006.05.008 Zimmerman, 1991, Two-stage autolysis of the catalytic subunit initiates activation of calpain I, Biochimica et Biophysica Acta: Protein Struct. Mol. Enzymol., 1078, 192, 10.1016/0167-4838(91)99009-H Parkes, 1985, Calpain inhibition by peptide epoxides, Biochem., 230, 509, 10.1042/bj2300509 Edmunds, 1991, Comparison of the autolyzed and unautolyzed forms of μ- and m-calpain from bovine skeletal muscle, Biochimica et Biophysica Acta: Protein Struct. Mol. Enzymol., 1077, 197, 10.1016/0167-4838(91)90059-9 Boehm, 1998, Changes in the calpains and calpastatin during postmortem storage of bovine muscle, J. Anim. Sci., 76, 2415, 10.2527/1998.7692415x Ono, 2004, Possible regulation of the conventional calpain system by skeletal muscle specific calpain, p94/calpain 3, J. Biol. Chem., 279, 2761, 10.1074/jbc.M308789200 García Díaz, 2006, Ca2+ Dependency of calpain 3 (p94) activation, Biochem., 45, 3714, 10.1021/bi051917j Kramerova, 2008, Novel role of calpain-3 in the triad-associated protein complex regulating calcium release in skeletal muscle, Hum. Mol. Genet., 17, 3271, 10.1093/hmg/ddn223 Kramerova, 2004, Null mutation of calpain 3 (p94) in mice causes abnormal sarcomere formation in vivo and in vitro, Hum. Mol. Gen., 13, 1373, 10.1093/hmg/ddh153 Sorimachi, 1995, Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence, J. Biol. Chem., 270, 31158, 10.1074/jbc.270.52.31158 Taylor, 1995, Proteolytic activity of proteasome on myofibrillar structures, Mol. Biol. Reports., 21, 71, 10.1007/BF00990974 Ono, 2010, Skeletal muscle-specific calpain is an intracellular Na+-dependent protease, J. Biol. Chem., 285, 22986, 10.1074/jbc.M110.126946 Parr, 1999, Skeletal muscle-specific calpain and variable post-mortem tenderization in porcine longissimus muscle, J. Anim. Sci., 77, 661, 10.2527/1999.773661x Ilian, 2001, Intermuscular variation in tenderness: Association with the ubiquitous and muscle-specific calpains, J. Anim. Sci., 79, 122, 10.2527/2001.791122x Geesink, 2005, Calpain 3/p94 is not involved in postmortem proteolysis, J. Anim. Sci., 83, 1646, 10.2527/2005.8371646x Lazarides, 1976, Immunological characterisation of the subunit of the 100 A filament from muscle cell, Proc. Natl. Acad. Sci. U. S. A., 73, 4344, 10.1073/pnas.73.12.4344 Paulin, 2004, Desmin: A major intermediate filament protein essential for the structural integrity and function of muscle, Exp. Cell Res., 301, 1, 10.1016/j.yexcr.2004.08.004 Christensen, 2004, Effect of muscle type on the rate of post-mortem proteolysis in pigs, Meat Sci., 66, 595, 10.1016/S0309-1740(03)00175-X Hwan, 1989, Studies of desmin and α-actinin degradation in bovine semitendinosous muscle, J. Food Sci., 54, 1426, 10.1111/j.1365-2621.1989.tb05126.x Kristensen, 2001, The effect of aging on the water-holding capacity of pork: role of cytoskeletal proteins, Meat Sci., 58, 17, 10.1016/S0309-1740(00)00125-X Morrisson, 1998, Immunolocalisation of intermediate filaments proteins in porcine meat. Fibre type and muscle-specificity variations during conditioning, Meat Sci., 50, 91, 10.1016/S0309-1740(98)00019-9 Verrez-Bagnis, 1999, Desmin degradation in postmortem fish muscle, J. Food Sci., 64, 240, 10.1111/j.1365-2621.1999.tb15873.x Kitamura, 2005, Mechanism of production of troponin T fragments during postmortem aging of porcine muscle, J. Agric. Food Chem., 53, 4178, 10.1021/jf047974l Baron, 2004, Cleavage of desmin by cysteine proteases: Calpains and cathepsin B, Meat Sci., 68, 447, 10.1016/j.meatsci.2004.03.019 Lametsch, 2004, Identification of myofibrillar substrates for μ-calpain, Meat Sci., 68, 515, 10.1016/j.meatsci.2004.03.018 Schafer, 2002, Physiological and structural events post mortem of importance for drip loss in pork, Meat Sci., 61, 355, 10.1016/S0309-1740(01)00205-4 Kemp, 2012, Advances in apoptotic mediated proteolysis in meat tenderisation, Meat Sci., 92, 252, 10.1016/j.meatsci.2012.03.013 Muroya, 2010, Desmin and troponin T are degraded faster in type IIb muscle fibers than in type I fibers during postmortem aging of porcine muscle, Meat Sci., 86, 764, 10.1016/j.meatsci.2010.06.019 Harris, 2001, Antioxidant status affects color stability and tenderness of calcium chloride injected beef, J. Anim. Sci., 79, 666, 10.2527/2001.793666x Penny, 1979, Relationship between toughness and troponin T in conditioned beef, Meat Sci., 3, 135, 10.1016/0309-1740(79)90015-9 Iwanowska, 2010, Changes in proteins and tenderness of meat from young bulls of four breeds at three ages over 10 days of cold storage, Anim. Sci. Papers Reports., 28, 13 Lana, 2016, Proteolysis in meat tenderization from the point of view of each single protein: A proteomic perspective, J. Proteomics, 147, 85, 10.1016/j.jprot.2016.02.011 Rowe, 2003, Effects of oxidation on beef tenderness and calpain activity, J. Anim. Sci., 81, 74 Sun, 2014, Prediction of troponin-T degradation using color image texture features in 10 d aged beef longissimus steaks, Meat Sci., 96, 837, 10.1016/j.meatsci.2013.09.012 Thomson, 2008, Length of exposure to high post-rigor temperatures affects the tenderisation of the beef M. Longissmus dorsi, Australian J. Exp. Agric., 48, 1442, 10.1071/EA07132 White, 2006, Manipulation of the pre-rigor glycolytic behaviour of bovine M-longissimus dorsi in order to identify causes of inconsistencies in tenderness, Meat Sci., 73, 151, 10.1016/j.meatsci.2005.11.021 Hwang, 2004, Effects of muscle shortening and proteolysis on Warner-Bratzler shear force in beef longissimus and semitendinosus, Meat Sci., 68, 497, 10.1016/j.meatsci.2004.04.002 Du, 2017, Phosphorylation inhibits the activity of μ-calpain at different incubation temperatures and Ca2+ concentrations in vitro, Food Chem., 228, 649, 10.1016/j.foodchem.2017.02.003 Mohrhauser, 2014, Calpain-1 activity in bovine muscle is primarily influenced by temperature, not pH decline, J. Anim. Sci., 2, 1261, 10.2527/jas.2013-7270 Pomponio, 2012, The effect of temperature on the activity of μ- and m-calpain and calpastatin during post-mortem storage of porcine Longissimus muscle, Meat Sci., 91, 50, 10.1016/j.meatsci.2011.12.005 Thompson, 1990, Effects of autolysis on the catalytic properties of the calpains, Biol. Chem. Hoppe-Seyler, 371, 177 Pomponio, 2008, Evidence for post-mortem m-calpain autolysis in porcine muscle, Meat Sci., 80, 761, 10.1016/j.meatsci.2008.03.019 Barbut, 2008, Progress in reducing the pale, soft and exudative (PSE) problem in pork and poultry meat, Meat Sci., 79, 46, 10.1016/j.meatsci.2007.07.031 Bee, 2007, Rate and extent of pH decline affect proteolysis of cytoskeletal proteins and water-holding capacity in pork, Meat Sci., 76, 359, 10.1016/j.meatsci.2006.12.004 Lametsch, 2008, Disulfide bond within mu-calpain active site inhibits activity and autolysis, Biochimica et Biophysica Acta-Proteins Proteomics., 1784, 1215, 10.1016/j.bbapap.2008.04.018 Chen, 2014, Influence of oxidation on the susceptibility of purified desmin to degradation by μ-calpain, caspase-3 and -6, Food Chem., 150, 220, 10.1016/j.foodchem.2013.10.149 Xue, 2012, Influence of oxidation on myofibrillar proteins degradation from bovine via μ-calpain, Food Chem., 134, 106, 10.1016/j.foodchem.2012.02.072 Rowe, 2004, Oxidative environments decrease tenderization of beef steaks through inactivation of μ-calpain, J. Anim. Sci., 82, 3254, 10.2527/2004.82113254x