Formations of Oligopeptides from Dipeptides by the Protease from Streptomyces cellulosae
1984 年 48 巻 5 号 p. 1231-1237
詳細
1984 年 48 巻 5 号 p. 1231-1237
The protease from Streptomyces cellulosae formed more turbidity in a 16% soybean protein hydrolysate in the initial stage of the reaction than α-chymotrypsin did, when the proteolytic activity of the protease was same as that of α-chymotrypsin. In highly concentrated solutions (2.5%) of various dipeptides, oligopeptides were produced by condensation by the protease. The oligopeptides formed were (L-Leu-Gly)2 and (L-Leu-Gly)3 from L-Leu-Gly, (L-Phe-L-Val)2 from L-Phe-LVal, (L-Val-L-Phe)2 and (L-Val-L-Phe)3 from L-Val-L-Phe, and (L-Leu-L-Met)2 and (L-Leu-L-Met)3 from L-Leu-L-Met.
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