Agricultural and Biological Chemistry
Online ISSN : 1881-1280
Print ISSN : 0002-1369
ISSN-L : 0002-1369
Studies on Proteolytic Enzymes of Streptomyces griseus
Part III. Some Properties of Alkaline Proteinase from Culture Media of Streptomyces griseus ATCC 3463
Takeshi OUCHI
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1962 Volume 26 Issue 11 Pages 734-739

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Abstract

The proteinase of Streptomyces griseus ATCC 3463 shows some characteristic properties different from other known proteolytic enzymes from genus Streptomyces. The optimal pH for reaction of this enzyme is 10.0 and the enzyme is stable around pH2.5 but labile at pHs from 3.5 to 7.5. The enzyme hydrolyzes various synthetic substrates for papain, trypsin and chymotrypsin, whereas it acts neither on carbobenzoxy-L-glutamyl-L-tyrosine, a synthetic substrate for pepsin, nor on twenty-four kinds of peptides and amino acid amides splitted by peptidase. The enzyme activity is not inhibited by metal chelating agents, and not activated by metal ion, indicating that it is not a metalloenzyme.

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