NDLI: Purification and Some Properties of a Protease fromStreptomyces cellulosae

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Purification and Some Properties of a Protease fromStreptomyces cellulosae

Content Provider	Scilit
Author	Muro, Tetsuo Tominaga, Yoshio Okada, Shigetaka
Copyright Year	1984
Description	We selected Streptomyces cellulosae bacause it secreted an unusual protease into the culture broth. The protease 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. The protease was purified 564-fold from culture broth in 5.8% yield. The precipitated product from the soybean protein hydrolysate was a protein-like compound containing mainly hydrophobic amino acids.
Related Links	https://www.tandfonline.com/doi/pdf/10.1080/00021369.1984.10866294?needAccess=true
Ending Page	1230
Page Count	8
Starting Page	1223
ISSN	09168451
e-ISSN	13476947
DOI	10.1080/00021369.1984.10866294
Journal	Bioscience, Biotechnology, and Biochemistry
Issue Number	5
Volume Number	48
Language	English
Publisher	Informa UK Limited
Publisher Date	1984-05-01
Access Restriction	Open
Subject Keyword	Paper and Wood Protein Protease Hydrophobic Proteolytic Chymotrypsin Fromstreptomyces Cellulosae
Content Type	Text
Subject	Organic Chemistry Medicine Analytical Chemistry Molecular Biology Biochemistry Applied Microbiology and Biotechnology Biotechnology

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