Thirty-five isolates belonging to the various genus of bacteria family were isolated from 25 different soil samples from various industrial areas from different districts of Tamil Nadu. One out of them were identified as P.aeruginosa (P1) and screened for pyocyanin production using submerged fermentation. The Pyocyanin production reached µg/ml on modified pseudomonas broth. The identification of strain was confirmed by 16s rRNA, the similarity with other strains available in the database was 98% (FDAARGOS_767). P1 was accessed at gene bank with accession number CP041008.1. Identification of the PhzM gene encoding PhzM enzyme was carried out using gene-specific primer followed by PCR. 190bp size gene was amplified using PCR. PhzM gene was confirmed and similarity with (FDAARGOS_767) strain was 100% in the database. Pyocyanin was extracted by standard chloroform extraction method, purified by HPLC (C17 column) and characterized by UV-Vis absorption spectroscopy, Particle size, zeta potential, FT-IR and LC-MS. The SEM analysis of pyocyanin pigment showed the particle size of microencapsulated pyocyanin. The cytotoxic effect of pyocyanin was investigated using VERO cells and it showed a concentration-response relationship between the concentration and cell viability the cytotoxicity increased gradually with the increase of its concentration.

Bioactive peptides have been defined as specific protein fragments that have an impact on body functions or conditions and may ultimately influence health. Fermented milk is a dairy product which has abundance of bioactive peptides. In this study, Casein Phospho peptide (CPP) was isolated by enzymatic hydrolysis of fermented milk using trypsin. The molecular weight of the Casein Phospho peptide was 3.5 KDa. The anti-bacterial activity of Casein Phospho peptide was determined using four pathogens such as, Escherichia coli, Bacillus cereus, Staphylococcus aureus and Salmonella enterica. Casein phospho peptide formed a zone of inhibition against the pathogens. The bioactive peptides were characterized using Fourier Transform Infra-Red Spectroscopy (FT-IR), Casein Phospho peptide had aliphatic amine, acetyl amino I and acetyl amino II functional groups. The HPLC analysis of Casein Phospho peptide revealed that the major amino acid present was L- Glutamic acid and the amino acid present in lesser concentration was Leucine. Peripheral Blood Mononuclear Cells (PBMCs) were isolated from human blood and the cells were treated with Casein Phospho peptide to assess the immunomodulatory effect. Casein Phospho peptide was able to produce a higher concentration of IL-10 anti-inflammatory cytokines when treated with PBMCs.

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