The influence of the rate of pH decline on the rate of ageing for pork. II: Interaction with chilling temperature
Introduction
Variations in temperature and pH decline post slaughter are believed to influence the rate of ageing of pork muscle post slaughter. In paper (I) we investigated the influence of pH decline rate on the rate of ageing of pork and the impact of pelvic suspension on improving post-slaughter tenderness. It was hypothesised that a fast rate of pH decline with a slow decline in muscle temperature will result in protein denaturation thereby preventing improvements in tenderness with post slaughter storage. It was also hypothesised that a slow rate of pH decline with a fast decline in muscle temperature will result in cold toughening thereby preventing improvements in tenderness with post slaughter storage. The final hypothesis was that an intermediate rate of pH and temperature decline will prevent protein denaturation and cold toughening and promote proteolytic activity thereby resulting in improvements in tenderness with post slaughter storage.
The aim of the experiment was to investigate the effect of the rate of pH and temperature decline in pork carcasses on the rate of change in tenderness with post slaughter storage.
Section snippets
Methodology
Twenty-four male Large White×Landrace finisher pigs were slaughtered over three slaughter days and randomly allocated to one of four treatments designed to alter the rate of pH decline. The average live weight of the pigs was 89.4±22.67 kg. This resulted in an average carcass weight of 64.6±18.14 kg and a fat depth at the P2 site of 19.7±6.9 mm. The stunning treatments were either electrical stunning using head to heart tongs (E, 1.3 amps for 4 s with variable voltage) or carbon dioxide
Results
No sides could be classified as DFD while 6 sides could be classified as PSE [n=2—stimulated for 60 s, chilled at 2 °C (33% of carcasses); n=2—stimulated for 60 s, chilled at 14 °C (33% of carcasses); n=1—stimulated 15 s, chilled 2 °C (16% of carcasses); n=1—stimulated 15 s, chilled at 14 °C (16% of carcasses)] using the definition of PSE and DFD described in Warner, Kauffman, and Russell (1993).
Results grouped according to rate of pH decline post slaughter
The results for the experiment described in part 1 (Rees et al., in press) and this experiment when grouped according to the rate of pH decline can be seen in Table 5.
The pH at 30 min, 1, 2 and 3 h post slaughter were all influenced by the rate of pH decline (P<0.05 for all) with the fast group having the lowest pH at each time with no differences in pH between the medium and slow groups. At 4, 5 and 6 h post slaughter the fast group had the lowest pH and the pH of the medium group was lower
Discussion
The treatments imposed in this experiment were designed to induce the extremes of protein denaturation and cold shortening. It was hypothesised that by inducing a rapid rate of pH decline with a slow rate of temperature decline, protein denaturation would occur, thus allowing the influence of protein denaturation on the rate of ageing to be determined. To induce variations in the rate of pH decline, electrical and CO2 stunning was employed as well as a short and long electrical stimulation
Acknowledgements
The authors wish to acknowledge the financial assistance of the Pig Research and Development Corporation, Canberra, Australia and the assistance of D. D'Souza, P. Walker, C. Hofmeyr, H. Channon, M. Kerr, A. Payne, R. Biden, P. Weston and K. Butler.
References (48)
- et al.
Comparison of CO2 stunning with mannual electrical stunning of pigs on carcass and meat quality
Meat Science
(2002) Optimisation of tenderisation, ageing and tenderness
Meat Science
(1994)- et al.
Modelling post mortem tenderisation—IIenzyme changes during storage of electrically stimulated and non-stimulated beef
Meat Science
(1992) - et al.
Effect of electrical stimulation, hip suspension and ageing on quality of chilled pig meat
Meat Science
(1991) - et al.
Modelling post mortem tenderisation—Itexture of electrically stimulated and non-stimulated beef
Meat Science
(1992) - et al.
Changes in solubility and enzymic activity of muscle glycogen phosphorylase in PSE muscles
Meat Science
(1979) - et al.
Factors affecting polyacrylamide gel electrophoresis and electroblotting of high molecular weight myofibrillar proteins
Analytical Biochemistry
(1989) - et al.
Determinants of tenderisation in beef longissimus dorsi and triceps brachii muscles
Meat Science
(1995) - et al.
Sarcomere shortening of prerigor muscle and its influence on drip loss
Meat Science
(1986) - et al.
Tenderisation of pork as affected by degree of cold-induced shortening
Meat Science
(1995)
Post slaughter influences on the formation of metmyoglobin in beef muscles
Meat Science
Effects of early post mortem glycolytic rate on beef tenderness
Meat Science
Calpains and calpastatin distribution in bovine, porcine and ovine skeletal muscles
Meat Science
Quadratic relationship between early postmortem glycolytic rate and beef tenderness
Meat Science
Correlations of sensory and instrumental meat tenderness values as affected by sampling techniques
Food Quality and Preference
Beef tenderness and sarcomere length
Meat Science
Effects of low frequency electrical stimulation on beef tenderness
Meat Science
The effect of low voltage and high voltage electrical stimulation on pork quality
Meat Science
Effects of low voltage electrical stimulation during exsanguination on meat quality and display colour stability
Meat Science
Muscle protein changes post mortem in relation to pork quality traits
Meat Science
Quality attributes of major porcine muscles: a comparison with the longissimus lumborum
Meat Science
The efficiency of high and low voltage electrical stimulation under different chilling regimes
Canadian Journal of Animal Science
Objective-subjective assessment of meat tenderness
Journal of Texture Studies
Effects of beef carcass electrical stimulation, hot boning and ageing on unfrozen and frozen longissimus dorsi and semimembranosus steaks
Journal of Food Science
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Present address Food Science and Nutrition, School of Biomolecular and Biomedical Science, Griffith University, Logan Campus Queensland 4111, Australia.