Purification and characterization of bacteriocin produced by oral Lactobacillus paracasei SD1.

The present study aimed to purify and characterize the antimicrobial protein from Lactobacillus paracasei SD1, which is a strain from the human oral cavity. Antimicrobial activity was obtained from purifying the culture supernatant of L. paracasei SD1. Purification of the active compound was achieved with ammonium sulfate precipitation followed by chloroform and gel filtration chromatography. As revealed by SDS-PAGE, the active fraction was homogeneous, showing a protein with an approximate molecular weight of 25,000 Da. It was confirmed as having a molecular mass of 24,028.2 Da by mass spectrometry. The antimicrobial compound, named "paracasin SD1", exhibited a broad spectrum against oral pathogens. Paracasin SD1 was stable in a pH range between 3.0 and 8.0 at 100 °C for 5 min, and showed resistance to α-amylase, catalase, lysozyme and whole saliva. However, its activity was lost after proteinase K and trypsin treatment. The results obtained suggest the possibility of using paracasin SD1 for application in prevention/treatment of oral diseases.