Abstract
Tenderness is a most desirable quality in meat; during the conversion of muscle to meat and its subsequent storage, endogenous enzyme activity is the main factor contributing to the development of tenderness.
Up to 24 hours after slaughter, anaerobic glycolysis in muscle generates lactic acid and lowers the pH. With adequate initial concentrations of glycogen the pH falls to about 5·5 whereupon glycolysis ceases, due mainly to inhibition of phosphofructokinase. If glycogen is depleted prior to slaughter, the ultimate pH may be as high as 7: such meat binds more water and is more tender than that at pH 5-5. During rigor mortis the level of A TP falls, causing the overlapping parts of actin and myosin filaments to combine; reducing the degree of overlap of actin and myosin increases tenderness.
Tenderisation is effected by storing beef for ten days at about 2°C, poultry is tenderised after only one day. In tenderised meat the Z-discs which interlock the actin filaments are fragmented, initially by a calcium-activated neutral protease. At lowpH, lysosomal cathepsins B and D contribute to myofibrillar breakdown. Release of cathepsins B and N (collagenolytic enzymes) into the extracellular spaces may weaken the intramuscular connective tissues. These glycolytic and auto lytic changes are discussed in relation to the commercial handling of meat.
Added tenderisers augment the action of the muscle enzymes and usually contain the plant protease, papain. Oxidised (deactivated) papain can be injected into the blood stream ante mortem or active papain can be applied to meat post mortem. The tenderising action of papain occurs predominantly during cooking.
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Dransfield, E., Etherington, D. (1981). Enzymes in the Tenderisation of Meat. In: Birch, G.G., Blakebrough, N., Parker, K.J. (eds) Enzymes and Food Processing. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-6740-6_10
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DOI: https://doi.org/10.1007/978-94-011-6740-6_10
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