SEARCHING AND IN SILLICO CHARACTERIZATION OF STREPTOMYCES PHAGE ENDOLYSINS AND THEIR CATALYTIC DOMAINS

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October – November, 2020, vol. 10, no. 2
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Article type: Biotechnology of Biotechnology
DOI: 10.15414/jmbfs.2020.10.2.221-229
Abstract: Endolysins, peptidoglycan hydrolases encoded by bacteriophages, degrade bacterial cell wall and are promising alternative to antibiotics. Howewer, the selection and bioengineering of endolysins needs previous bioinformatic characterization. This study focuses on endolysins encoded by viruses infecting Streptomyces spp., describes Streptomyces phages diversity and association. Set of 143 endolysins were predicted in 175 Streptomyces phage genomes from NCBI database and The Actinobacteriophage Database and were characterized their phylogeny and function domains, especially catalytic domains. Predicted endolysins have amidase (Ami_2 and CHAP domain), muramidase (glycol_hydro_25) and peptidase activity (CHAP, NlpC/P60). This bioinformatic characterization serve as a base to next research in developing of endolysins with new properties in enzybiotik form.
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