A novel serine protease from pseuderanthemum latifolium B. Hansen: Characterization and fibrino(geno)lytic activities

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

Keywords:

• Pseuderanthemum latifolium
• serine protease
• amino acid sequence
• characterization
• fibrino(geno)lytic activity

Disclosure statement

The authors declare no competing financial interest

Additional information

Funding

This research was funded by Vietnam National Foundation for Science and Technology Development (NAFOSTED) under grant number 106-NN.02-2015.54 and the International Foundation for Science, Stockholm, Sweden, through a grant N° F/5371-1.