List of Lactiplantibacillus Plantarum Strains' Surface Proteins for the Dairy and Vegetable Niches

Abstract

With its pertinent probiotic and technological characteristics, Lactiplantibacillus plantarum (previously
Lactobacillus plantarum) is employed extensively in the food industry to enhance the flavor, texture,
and organoleptic qualities of fermented goods. As the primary players in bacterial-host interactions,
cell-surface proteins play a crucial part in the molecular processes that produce beneficial effects. In
order to obtain a complete picture of variations in protein profiles that might be connected to the
strains' particular characteristics and habitat of origin, the proteins found on the surface of four L.
plantarum strains—two of which were isolated from vegetable matrices and two from dairy products—
were identified using proteomics. The findings showed that strains from vegetable matrices had a more
varied pattern of surface proteins than bacteria from dairy matrices (>500 proteins vs. roughly 200
proteins, respectively). A core of 143 proteins was shared by the four strains, although 445 of those
proteins were unique to strains derived from vegetable matrices, while 26 were unique to strains
originating from dairy. Only strains from vegetable matrices exhibited choloylglycine hydrolase (bile
salt hydrolase) and sortase A, which are involved in adhesion. These strains, especially L. plantarum
S61, may offer substantial probiotic and biotechnological promise based on the unusual molecular
activities of the discovered proteins.