Abstract Protease (PPL) was isolated from Pseuderanthemum latifolium B. Hansen and had a molecular mass of 70 kDa. The N-terminal sequence of PPL showed 70-80% similarity with of subtilisin-like serine proteases from plants, but it did not show any sequence homology with known plant proteases. Serine protease inhibitors (PMSF, DFP) effectively blocked about 90% of PPL activity. PPL was highly activity at the pH range from 6 to 9 and temperatures from 50 °C to 80 °C, with an optimum at pH 7.0 and temperatures 70 °C. PPL had stability in a variety of pH, temperature, surfactant and oxidizing agents. PPL with concentration of 2.5 µg completely hydrolyzed the Aα-chain of fibrinogen within 5 min and hydrolyzed the Bβ and the γ-chain after 10 h. Fibrin also was strong hydrolyzed by PPL with concentration of 0.3 µg. Thus, PPL is a unique serine protease, which it had strong fibrino(geno)lytic activities. GRAPHICAL ABSTRACT
A novel serine protease from pseuderanthemum latifolium B. Hansen: Characterization and fibrino(geno)lytic activities
L. Truong,B. Paulsen,Vo Hoai Bac
Published 2019 in Natural Product Research
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- Publication year
2019
- Venue
Natural Product Research
- Publication date
2019-08-23
- Fields of study
Biology, Medicine, Chemistry
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Semantic Scholar, PubMed
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