• Applied Biological Chemistry
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• v.15 no.2
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• pp.111-142
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• 1972

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 $4{\sim}9$ 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. [P]-I. Pro (Cys Ala Asp Trp Ile Val) Glu [P]-II. Val (His Arg Glu Thr Ala Met) Asp [P]-III. Glu (Cys Lys Asp Thr Met) Ala [P]-IV. Glu(His Ser Ala) Met) [P]-V. Ile (Cys Asp Arg Gly Pro T.p Phe) His [P]-VI. Gly(Asp ser) Lys [P]-VII. Thr(Pro Tyr Phe) Asp [P]-VIII. Phe(Tyr Leu Ile) Val [P]-IX. Trp (Phelle) Thr [P]-X. Ile (Arg Leu) Phe [P]-XI. Asp (Lys His Ser Gly Glu Pro) Ala [P]-XII. Glu (Cys Asp Gly) Ser [P]-XIII. Ala (Arg Tyr) Glu [P]-XIV. Met (Glu Ala) His It appears that the protease of the Bacillus subtilis K-27 syrain has rather wider range of specificity than proteases of Aspergoillus soya, pepsin, chymotrypsin, and trypsin.