Production, Purification and Characterisation of a Potential Fibrinolytic Protease from Endophytic Xylaria curta by Solid Substrate Fermentation.
Appl Biochem Biotechnol
; 181(4): 1496-1512, 2017 Apr.
Article
en En
| MEDLINE
| ID: mdl-27787769
ABSTRACT
The present investigation highlights the optimal conditions for production of a non-toxic, bi-functional fibrinolytic enzyme xylarinase produced by endophytic fungus Xylaria curta by solid substrate fermentation using rice chaff medium. The purified enzyme is a monomeric protein with a molecular mass of â¼33 kDa. The enzyme exhibits cleavage of Aα and Bß chains of fibrin(ogen) and has no effect on γ chain. The optimal fibrinolytic activity of the enzyme was observed at 35 °C and pH 8. The fibrinolytic activity was enhanced in the presence of Ca2+, whereas it was completely inhibited in the presence of Fe2+ and Zn2+ ions and inhibitors like EDTA and EGTA suggesting it to be a metalloprotease. The K m and V max of the enzyme for azocasein were 326 µM and 0.13 µM min-1. The N-terminal sequence of the enzyme (SNGPLPGGVVWAG) was same when compared to xylarinase isolated from culture broth of X. curta. Thus, xylarinase could be exploited as a potent clot busting enzyme which could be produced on large scale using solid substrate fermentation.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Xylariales
/
Proteínas Fúngicas
/
Fermentación
/
Endófitos
/
Fibrinólisis
/
Metaloproteínas
Límite:
Animals
Idioma:
En
Revista:
Appl Biochem Biotechnol
Año:
2017
Tipo del documento:
Article
País de afiliación:
India