Inhibitory modes of Kunitz and Bowman-Birk soybean trypsin inhibitors to tryptic and chymotryptic proteinases of tiger puffer and yellowtail

SUMMARY: An inhibitory effect of Kunitz and Bowman-Birk soybean trypsin inhibitors (K- and BB-SBTI) was investigated on tryptic and chymotryptic proteinases of a brood of tiger puffer Takifugu rubripes and yellowtail Seriola quinqueradiata. These assist to comprehend the differences in dietary soybean meal (SBM) utility by fish species and to develop low cost SBM diets with low contents of fish meal. The K-SBTI strongly inhibited tryptic proteinase and weakly inhibited chymotryptic proteinase from the hepatopancreas and intestine including pyloric ceca of the fishes. The BB-SBTI strongly inhibited both proteinases of the fishes. The K-SBTI inhibition for tryptic protease and the BB-SBTI inhibition for tryptic and chymotryptic proteases were relatively constant in tiger puffer with growth of 12–199 g bodyweight. In yellowtail with growth of 7–672 g bodyweight, the K-SBTI inhibition for tryptic protease and the BB-SBTI inhibition for chymotryptic protease were also relatively constant. The BB-SBTI inhibition for yellowtail tryptic protease typically fell in the stage from 7 g to 57 g bodyweight, and then decreased slightly or was maintained constantly. These results indicate that there are different inhibitory modes of K- and BB-SBTI and there is inter- and intraspecific diversity of tryptic protease conformation between the two species.