Excessive meat tenderization in cured raw Parma ham has recently been
correlated with abnormal levels of cathepsin B in freshly slaughtered
thigh meat. We have developed a visual assay employing the substrate Z
-Arg-Arg-NNapOMe for the quantitative detection of active cathepsin B
levels in pork thigh muscle homogenates. The work was based on a kinet
ic characterization, in steady state condition, of pig muscle cathepsi
n B with several peptidyl chromophoric substrate analogs. This assay c
an easily and safely be performed by non-specialized personnel directl
y in the slaughterhouse or in the factory, for an early quality evalua
tion of thighs selected for Parma ham production. Our characterization
has further indicated that the catalytic properties of porcine muscle
cathepsin B and those of isoforms from other animal and plant species
are practically identical. This is particularly evident in the commer
cially available bovine spleen isoform, which was employed as a model
enzyme in most of the experiments. (C) 1997 Elsevier Science Ltd.