Comparison of Proteolytic Enzyme Levels in Chicken, Pig, Lamb and Rabbit Muscle at Point of Slaughter: Role in Meat Tenderisationpost mortem
✍ Scribed by Blanchard, Paul J; Mantle, David
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 940 KB
- Volume
- 71
- Category
- Article
- ISSN
- 0022-5142
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✦ Synopsis
In order to develop a clearer understanding of the biochemical mechanism underlying the process of meat tenderisation, a comparison was made of the levels of a comprehensive range of protein catabolising proteolytic enzymes in muscle from animal species known to differ markedly in rates of meat tenderisation, ie chicken (breast and thigh muscles), pig, lamb and rabbit (longissirnus dorsi muscles). Proteolytic enzyme activities were determined at point of slaughter: (i) for the following protease types using optimized specific fluorimetric assays: alanyl-, arginyl-, leucyl-, and pyroglutamyl aminopeptidases, dipeptidyl aminopelptidases I11 and IV, tripeptidyl aminopeptidase, proline endopeptidase, calpain and macropain (cytoplasmic proteases); dipeptidyl aminopeptidases I and 11, cathepsins B, D H and L (lysosomal proteases)); (ii) using tissue homogenate time course assays to measure rates of structural protein degradation (via analytical electrophoresis) by endogenous cytoplasmic or lysosomal proteases. Although chicken (the most rapidly tenderising) muscles contained the highest levels of activity for most proteases measured, there was no general relationship between muscle proteolytic capacity and previously published meat tenderisation rates for the other species investigated. It would therefore appear that known differences in the rate of tenderisation in different species cannot be rationalised solely in terms of species specific differences in muscle proteolytic capacity and, whilst the latter is of importance in the tenderisation process, other potential factors should be taken into consideration.