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Journal of Chemistry
Volume 2015 (2015), Article ID 963041, 9 pages
Research Article

Streptomyces lavendulae Protease Inhibitor: Purification, Gene Overexpression, and 3-Dimensional Structure

1Microbiology Department, National Center for Radiation Research and Technology (NCRRT), 3 Ahmed El-Zomor Street, 8th Sector, Nasr City, Cairo 11371, Egypt
2Microbial Chemistry Department, National Research Centre (NRC), El-Bohouth Street, P.O. Box 12622, Dokki, Cairo, Egypt

Received 12 April 2015; Accepted 5 July 2015

Academic Editor: Ioannis G. Roussis

Copyright © 2015 D. E. El-Hadedy et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Protease inhibitors trypsin (STI1, Streptomyces trypsin inhibitor 1) has been identified, purified by ammonium sulfate precipitation and Sephadex G-100 gel filtration. SDS-PAGE of protease inhibitor showed molecular weight of approximately 10 KDa. PCR product (~1615 bp) of sti1 gene was cloned in expression vector pACYC177/ET3d and transformed in Escherichia coli JM109. Protease inhibitors trypsin was purified and used as antivirus against Coxsackievirus B3 (CVB3). CVB3 is one of the major causative agents of chronic, subacute, acute, and fulminant myocarditis as well as pancreatitis and aseptic meningitis. It has been reported that more than 50% of human myocarditis is associated with CVB3 infection.