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A novel fibrinolytic protease from Streptomyces sp. CS684

Paper ID Volume ID Publish Year Pages File Format Full-Text
35214 45081 2010 6 PDF Available
Title
A novel fibrinolytic protease from Streptomyces sp. CS684
Abstract

A fibrinolytic protease (FP84) was purified from Streptomyces sp. CS684, with the aim of isolating economically viable enzyme from a microbial source. SDS-PAGE and fibrin zymography of the purified enzyme showed a single protein band of approximately 35 kDa. Maximal activity was at 45 °C and pH 7–8, and the enzyme was stable between pH 6 and 9 and below 40 °C. It exhibited fibrinolytic activity, which is stronger than that of plasmin. FP84 hydrolyzed Bβ-chains of fibrinogen, but did not cleave Aα- and γ-chains. Km, Vmax and Kcat values for azocasein were 4.2 mg ml−1, 305.8 μg min−1 mg−1 and 188.7 s−1, respectively. The activity was suppressed by Co2+, Zn2+, Cu2+ and Fe2+, but slightly enhanced by Ca2+ and Mg+2. Additionally, the activity was slightly inhibited by aprotinin and PMSF, but significantly inhibited by pefabloc, EDTA and EGTA. The first 15 amino acids of N-terminal sequence were GTQENPPSSGLDDID. They are highly similar to those of serine proteases from various Streptomyces strains, but different with known fibrinolytic enzymes. These results suggest that FP84 is a novel serine metalloprotease with potential application in thrombolytic therapy.

Keywords
Fibrinolytic; Purification; Serine metalloprotease; Streptomyces; Thrombolytic therapy
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A novel fibrinolytic protease from Streptomyces sp. CS684
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 45, Issue 1, January 2010, Pages 88–93
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
Price after discount Only $4.95
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Full-text PDF Download
Online Support
Any Questions? feel free to contact us