NDLI: Production, Purification and Characterisation of a Potential Fibrinolytic Protease from Endophytic Xylaria curta by Solid Substrate Fermentation

Content Provider	Springer Nature Link
Author	Meshram, Vineet Saxena, Sanjai Paul, Karan Gupta, Mahiti Kapoor, Neha
Copyright Year	2016
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 ∼33 kDa. The enzyme exhibits cleavage of Aα and Bβ 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 Ca$^{2+}$, whereas it was completely inhibited in the presence of Fe$^{2+}$ and Zn$^{2+}$ 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.
Starting Page	1496
Ending Page	1512
Page Count	17
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	181
Issue Number	4
e-ISSN	15590291
Language	English
Publisher	Springer US
Publisher Date	2016-10-27
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Metalloprotease Solid-state fermentation Thrombosis Fibrinolysis Xylaria Biotechnology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

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