Liha töötlemine
than beef due to greater activation of the lation of μ- and m-calpain activity or be a
calpain system (Lee et al. 2008). negative regulator of apoptosis (Goll et al.
Ubiquitous μ- and m-calpains are het- 2003).
erodimers that dissociate in the presence of Less than 10% of total calpain is normally
Ca2+ into a regulatory 28 kDa subunit that is activated in the skeletal muscle (Goll et al.
identical in both isoforms (Carafoli and 2003). Research has demonstrated that the
Molinari 1998) and into a large catalytic optimal condition for calpain activity is pH
subunit (∼80 KDa). It is the catalytic subunit 7.5 at 25°C (Zeece et al. 1986), but activity
(Dutt et al. 2002) that dictates the Ca2+ level is still detected at pH 5. Meat tenderization
for activation. The μ- and m-calpains are begins at about pH 6.3 (approximately 6 h
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