Study on the Biochemical Mechanism of Degrading Keratins by Streptomyces fradiae
- VernacularTitle:链霉菌降解角蛋白的生化机制研究
- Author:
Lin HUANG
;
Zhi-Qiang XIONG
;
Hua-Jing CAI
;
Mei-Jin GUO
;
Guo-Quan TU
;
- Publication Type:Journal Article
- Keywords:
Streptomycec fradiae,Keratinase,Biochemical mechanism
- From:
Microbiology
1992;0(04):-
- CountryChina
- Language:Chinese
-
Abstract:
The biochemical mechanism of degrading keratins by S.fradiae var S-221 was primarily studied.The compounds (Na_ 2 SO_ 4 , Na_ 2 SO_ 3 and sulfdryl acohol), which respecitively enhance specific activity of keratinase, activate keratinase intensively and mainly act on the disulfide bonds reductase in the keratinase, Na_ 2 SO_ 3 activates intensively both disulfide bonds reductase and polypeptide hydrolytase at 0.01 mol/L, whereas Na_ 2 S_ 2 O_ 3 , which acts on the disulfide bonds reductase, inhibits keratinase.On the condition that substrate, keratins exists, S.fradiae var S-221 is induced to produce exo-keratinase, which is a multiproteinase, containing disulfide bonds reductase, which is a key enzyme degrading keratins, then, with polypeptidic, hydrolytase, graduately hydrolyzates denatured keratins into polypeptides, oligopeptides and free amino acids, so that keratins have been decomposed completely.Sulfur in the keratins was transferred into sulfhydryl compounds, H_ 2 S and sulfates in the course of keratinolysine.
