Three types of proteinases, namely cystein-, metallo-, and serine-proteinases were found in squid hepatopancreas by studying the inhibition spectra using carp myofibril as substrates. Cystein-, metallo-, and serine-type showed the highest activities at 50 ºC, 35 ºC, and 40 ºC, respectively. The optimal pHs were pH 5, pH 7, and pH 9 for cystein-, metallo-, and serine-type, respectively. When assayed at 20 ºC and pH7.5, metallo-type showed the highest activity. Metallo-type was characterized by a high selectivity in the digestion of myosin. Among the three enzymes, cystein-type was found to be the most stable against thermal and acid treatments. Heat treated myofibrils were more susceptible to cystein-and serine-types, but less susceptible to metallo-type. Acid treatment of myofibrils also enhanced the digestibility by cystein-type. The results indicated that cystein-type seemed to be the most suitable enzyme to produce peptides from denatured myofibrils by their random digestion.
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