The development of meat tenderness is likely to be compartmentalised by ultimate pH.
Bull Musculus longissimus dorsi (n=63) were categorised into high (pH≥6.2), intermediate (pH 5.8-6.19) and low (≤5.79) ultimate pH (pHu) and aged up to 28 days post mortem at -1°C. High pHu samples were acceptably tender at 1 day post mortem and significantly more tender than low pHu meat at all ageing timepoints (p<0.05). Rapid autolysis of μ-calpain in high pHu meat was linked with the more rapid degradation of titin, nebulin and filamin in this pHu group. Desmin degraded faster in low pHu meat and was concurrent with an increase of cathepsin B levels. The results from this study support the hypothesis that beef tenderisation is pHu compartmentalised with tenderness in high and low pHu meat characterised by variable rate of degradation of high and low molecular weight myofibrillar proteins during ageing, which are in turn regulated by μ-calpain and cathepsin B activities.
Food Assurance and Meat Quality, AgResearch Limited., Ruakura Research Centre, Private Bag 3123, Hamilton, New Zealand.
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D
Lomiwes
M M
MM
Farouk
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G
Wu
O A
OA
Young
D000818:Animals; D001329:Autolysis / Q000378:metabolism; D002154:Calpain / Q000378:metabolism; D002401:Cathepsin B / Q000378:metabolism; D002417:Cattle; D064211:Connectin / Q000378:metabolism; D003893:Desmin / Q000378:metabolism; D004044:Dietary Proteins / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D064448:Filamins / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008460:Meat / Q000032:analysis*; D009124:Muscle Proteins / Q000378:metabolism; D018482:Muscle, Skeletal / Q000737:chemistry; D009210:Myofibrils / Q000737:chemistry; D059748:Proteolysis
D064211:Connectin; D003893:Desmin; D004044:Dietary Proteins; D064448:Filamins; D009124:Muscle Proteins; C035620:nebulin; D002154:Calpain; C449002:mu-calpain; D002401:Cathepsin B
Beef; Cathepsin B; Compartmentalisation; Tenderness; Ultimate pH; μ-Calpain