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Purification and characterization of a novel, highly potent fibrinolytic enzyme from Paecilomyces tenuipes

Paper ID Volume ID Publish Year Pages File Format Full-Text
35247 45083 2011 9 PDF Available
Title
Purification and characterization of a novel, highly potent fibrinolytic enzyme from Paecilomyces tenuipes
Abstract

A fibrinolytic enzyme (PTEFP) was purified from the entomopathogenic fungus Paecilomyces tenuipes. Analysis of the purified PTEFP by SDS–PAGE and fibrin zymography demonstrated a single protein band of approximately 14 kDa. Fibrinolysis pattern showed that PTEFP rapidly hydrolyzed α-chain followed by β-chain. PTEFP rapidly degraded Aα-chain of human fibrinogen but did not hydrolyze Bβ- or γ-chain indicating that it is α-fibrinogenase. The N-terminal sequence was AQNIGAVVNLSPPKQ, which is different from that of other known fibrinolytic enzymes. The PTEFP displayed maximum activity at 35 °C and pH 5.0, and was stable between pH 5.0–8.0 and below 40 °C. Calcium ion enhanced the enzyme activity whereas Zn2+ inhibited it. The fibrinolytic activity was strongly inhibited by PMSF identifying it as a serine protease. PTEFP exhibited high specificity for the substrate H-D-Val-Leu-Lys-pNA and Km and Vmax values for this substrate were 0.17 mM and 59 U/ml respectively. These results suggest that PTEFP is a novel fibrinolytic enzyme and may have potential applications in treating thrombosis.

Keywords
Paecilomyces tenuipes; Fibrinolysis; Fungal enzymes; Thrombosis
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Purification and characterization of a novel, highly potent fibrinolytic enzyme from Paecilomyces tenuipes
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 46, Issue 8, August 2011, Pages 1545–1553
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
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