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Updated: Jul 26, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Screening and search for novel inhibitors of DD-peptidase 64-575
1Department of Actinomycetes and Fungi Imperfecti, National Institute of Hygiene (NIH), 24 Chocimska Str., 00-791 Warsaw, Poland.
Abstract:
The aim of the work was search for inhibitors of PBPs (penicillin binding proteins, DD-carboxypeptidase/transpeptidase, DD-peptidase). Between 141 tested Streptomyces strains, 25% showed activity of inhibitors production. The inhibitors were produced by selected Streptomyces strains (NIH Culture Collection). The culture supernatants of Streptomyces rimosus B PZH (inhibitor B) and Streptomyces rimosus NRRL 2234 (inhibitor 2234) exhibited the highest inhibition activity. Both inhibitors were purified by the use of: anion exchange chromatography and reversed phase chromatography (HPLC). Inhibitor B is a gamma-lactam compound and inhibitor 2234 is a beta-lactam.

