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Modelling post-mortem tenderisation-II: Enzyme changes during storage of electrically stimulated and non-stimulated
E Dransfield1, D J Etherington, M A Taylor
1Department of Veterinary Medicine, University of Bristol, Churchill Building, Langford, Bristol BS18 7DY, UK.
Meat Science
|November 9, 2011
Summary
Beef tenderness is linked to calpain I activity, which decreases faster at higher temperatures during storage. Lysosomal enzyme levels remained stable, while calpain II levels slightly decreased.
Area of Science:
- Meat Science
- Biochemistry
- Food Technology
Background:
- Proteolytic enzymes play a crucial role in meat tenderization.
- Calpains are key enzymes involved in post-mortem muscle changes.
- Understanding enzyme activity under different storage conditions is vital for meat quality.
Purpose of the Study:
- To investigate the impact of storage temperature on calpain I, calpain II, cathepsins, and β-glucuronidase activity in beef.
- To determine the relationship between calpain I degradation and beef tenderization rates.
- To assess the stability of lysosomal enzymes during meat storage.
Main Methods:
- Beef M. Pectoralis profundus samples were subjected to electrical stimulation or control conditions.
- Meat was stored at temperatures ranging from 0 to 30°C to prevent muscle shortening.
- Enzyme activity (calpains I and II, cathepsins B and L, β-glucuronidase) was measured in extracts over time.
Main Results:
- Lysosomal enzyme levels remained stable throughout storage.
- Calpain II levels showed a slight decrease with ageing and were unaffected by initial treatments.
- Calpain I activity decreased significantly at higher temperatures (accelerated loss above pH 6.2), with decay rates correlating to tenderization rates.
Conclusions:
- Calpain I degradation rate is directly linked to the rate of beef tenderization.
- Storage temperature significantly influences calpain I stability and meat tenderization.
- Lysosomal enzymes and calpain II are less critical factors in temperature-dependent tenderization compared to calpain I.
