P. Ertbjerg et al., Relationship between proteolytic changes and tenderness in prerigor lacticacid marinated beef, J SCI FOOD, 79(7), 1999, pp. 970-978
A meat tenderising procedure involving injection of a lactic acid solution
into prerigor muscle was investigated using beef M pectoralis profundus. Th
e distribution of lysosomal enzymes in subcellular fractions, densities of
myofibrillar protein bands after SDS-PAGE and shear force were measured in
non-injected, 0.5 M and 1.0 M lactic-acid-injected samples during a 21 days
ageing period. The activities of cathepsin B + L and beta-glucuronidase in
the soluble fraction increased with level of lactic acid and with time pos
t-mortem (P < 0.001). Lactic acid and storage decreased densities of SDS-PA
GE bands migrating at the position of myosin heavy chain (MHC) and alpha-ac
tinin and increased densities of a 150 kDa band (P < 0.01). SDS-PAGE of iso
lated perimysium cleaved with CNBr showed proteolytic cleavage of collagen
after prolonged storage. Lactic acid injection significantly reduced shear
force (P < 0.001). The cathepsin B + L activity in the soluble fraction cor
related to shear force (r = -0.8), the degradation of MHC and alpha-actinin
(r = -0.88 and -0.90) and the generation of the 150 kDa fragment (r = 0.90
) but not to the generation of a 31 kDa fragment (r = 0.05). A major part o
f the tenderness improvement after lactic acid injection was complete at 24
h post-mortem, and was therefore due to a rapid process, eg pa-induced swe
lling of the muscle structure. The data on enzyme activities and protein de
gradation, however, suggested that the action of lysosomal cathepsins also
contributed to textural changes. (C) 1999 Society of Chemical Industry.