An experimental Chung-Kook-Jang was prepared using the strain Bacillus subtilis sp. isolated by the author. Samples were taken in 12 hrs interval during the fermentation and the oligopeptides were separated by the method of molecular sieving using the ion exchange resin column of Dowex-50. Only the X-16 fraction of oligopeptides was taken and the components of oligopeptides were developed in two dimensional thin layer chromatograms. The each peptide spot was eluted and each peptide was isolated. The pattern and kinds of amino acids, and N and C-terminal amino acids were studied. Fourteen different oligopeptides could be detected by the two dimensional thin layer chromatography, all of which were consisted of 4∼9 kinds of amino acids. No dipeptides and no tripeptides could be found. The N and C-terminal amino acids and the residual component amino acids of all these 14 peptides could be summarized as the follows. 도표 It appears that the protease of the Bacillus subtilis K-27 strain has rather wider range of specificity than the proteases of Aspergoillus soya, pepsin, chymotrypsin, and trypsin.