These investigations were performed to clarify the effects of the alkaline protease purified from white muscle of carp, Cyprinus carpio and its potent inhibitors upon the "Modori" phenomenon in Kamaboko prepared from carp white muscle . The enzymatic activity was not inhibited by chicken egg white, soybean trypsin inhibitor, carp plasma, TLCK or t-AMCHA, but was considerably inhibited by leupeptin, ovomucoid, TPCK, antipain, K3, NEM and NBS. Therefore, the enzymatic properties of this protease

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... eem to be similar to those of a-chymotrypsin. The degree of "Modori" of Kamaboko prepared from the washed muscle was considerably less than that from the unwashed muscle, though about 70% of the enzymatic activity still remained in the washed muscle. This result could be explained by the inhibitory effect of added sodium chloride on the enzymatic activity. However, the "Modori" phenomenon in Kamaboko prepared from the unwashed muscle was not prevented by the addition of enzyme inhibitors such as K3, NEM, or NBS, and only partially by leupeptin. And also the elasticity of Kamaboko prepared from the muscle which was treatd to remove most of the enzyme and sarcoplasmic proteins was not reduced by the addition of the enzyme. From these results it may be concluded that the enzyme in muscle does not take part in the "Modori" phenomenon in Kamaboko production. * The molecular weight was calculated as propionyl-L-leucyl-L-leucyl-DL-argininal. The molecular weights of ovomucoid and STI were taken to be 27,000 and 20,000 respectively.