Purification, HR-LC-ESI-MS-MS Identification, and Peptide Prediction of Bacteriocin-Like Inhibitory Substances Produced by Streptomyces sp. Isolated from Chanos chanos.

Abstract

Consumption of fresh and minimally processed food is closely related to foodborne diseases. To minimize the adverse effects, bacteriocin-like inhibitory substance (BLIS) as a natural preservative can be used. One of the bacteriocins with promising activity was produced by Streptomyces sp. Using gel filtration chromatography, the bacteriocin purification process succeeded in obtaining semi-purified fractions with broad-spectrum inhibitory activity to foodborne pathogen bacteria. These fractions are also stable up to 100 °C and pH 2.0–7.0. High-Resolution Liquid Chromatography Electrospray Ionization-Tandem Mass Spectrometry analysis followed by orthogonal projection to latent structure showed that each fraction had eight peaks with the highest positive correlation to BLIS-specific activity. Peptide identification based on MS spectrum found 597 predictive peptides, of which 42 predictive peptides with antimicrobial peptide characteristics and the highest iAMPpred antimicrobial peptide probability (>0.5) were selected. The selected predictive peptides have molecular mass of 247.13-615.37 Da and consist of at least 20% hydrophobic amino acids with a hydrophobicity value of 14.72 Kcal mol−1. The results of this study indicate the effectiveness of BLIS purification by gel filtration chromatography and the promising potential of semi-purified BLIS as a natural preservative. Besides, the active peptides in semi-purified BLIS can also be identified quickly so that the isolation process to obtain purified-BLIS can be carried out more efficiently.