Studies on Bonito Pepsin-I

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Abstract
The gastric proteases of fishes have been studied in detail regarding enzyme properties. In the present paper, the purification method of the bonito pepsin was studied as a first step in the investigations to explain the enzymic characteristics of gastric proteases. When the extraction methods of pepsin from gastric mucosa of bonito were tested by using distilled water, acid solution (0.05 N HCl, pH 2.0), alkaline solution (0.4M Na-acetate-0.4M Na-carbonate, pH 8.1) and 25% acetone water solution, distilled water extraction proved to give the best yield. The pepsin purified by the modified method (Fig. 1) of Norris and Mathies (1953) had the specific activity of 0.198 [PU]HbmgPN which was 68 times as much as the original crude extract. From results of electrophoresis on starch gel (pH 3.2, 0.05M citrate buffer), it was ascertained that the hog crystallized pepsin showed only a spot migrating toward the anode. However, pepsin and the protease extracted from the gastric content of bonito showed two spots which migrated toward the cathode and were situated at approximately the same position. The bonito pepsin apparently differed from the hog crystallized pepsin in its electrophoretic behaviour.

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