Inferencia de secuencias codificantes de enzimas proteolíticas producidas por cepas bacterianas previamente aisladas de composta.

Abstract

Thermostable proteases are very important for the improvement of industrial processes; however, few efforts have been made in prospecting new enzymes from microorganisms in Ecuador. This study aimed to identify proteolytic activity of thermophilic bacterial strains previously isolated from compost and infer the coding sequences of those enzymes through genomic and phenotypic characterization. Three isolates out of twenty-showed proteolytic activity at 55 °C, in LB media enriched with skimmed milk. The genetic diversity and phylogeny of the proteolytic-thermophilic bacterial strains were determined by analyzing 16S rRNA sequences. Bacterial strains were classified as closely related to Bacillus subtilis and Bacillus thermoamylovorans. Additionally, the whole genomes of two proteolytic strains were sequenced and annotated. We identified five coding sequences associated with extracellular proteases potentially responsible for enzymatic activities observed in the phenotypic assays: Minor extracellular protease (Epr), Extracellular metalloprotease (mpr), Minor extracellular protease (vpr), Bacilopeptidase F (bpr), and Neutral protease B (nprb).