Conditioning of meat from different species. Relationship between tenderising and the levels of cathepsin B, cathepsin L, calpain I, calpain II and β-glucuronidase.

The conditioning times for beef, calf, lamb, pig and chicken M. pectoralis profundus were determined from extensibility measurements at 15°C. Extracts from the same muscle from these animals and also rabbit were assayed for free and total cathepsin activities using a new method to determine the extent of inhibition by cystatins. A new method was also developed for the rapid estimation of each calpain. The results show that pig muscle contained most cathepsin activity. Cathepsin L appeared to be inhibited to a greater degree than cathepsin B in the pig, rabbit and chicken muscle extracts. These extracts also contained proportionately more cathepsin L than the other species. Chicken muscle contained only a low level of the more sensitive neutral proteinase, calpain I. It was concluded that the rapid conditioning time for chicken muscle could not be explained in terms of either the free or total levels of cathepsins B and L, nor of the individual calpain activities.