Proteolytic Degradation of Salivary Proteins by Oral Streptococcus: Purification of Proteolytic Enzyme from S.oralis to Cleavage Human Salivary Mucin

Streptococcus oralis is a gram positive bacterium spherical or ovoid cocci, arranged in pairs and chains during growths itbelongsto the family Streptococcaceae, it has thick cell wall. The cell wall of the species contained ribitol and choline, but lacked rhamnose, and possessed directly cross-linked peptidoglycan with lysine as the diamino acid. S.oralis, a commensal species of the human oral cavity, belongs to the Mitis group of Streptococci that includes one of the major human pathogens, its a high-level penicillin and multiple antibiotic-resistant. S.oralishas emerged as one of the most important organisms of the viridians Streptococcus group in terms of infections and is recognized as an agent of Infective Endocarditis, Dental Plaqueand Blood Septicemia. S.oralis have avirulence factors such as adhesion, choline, proteolytic enzyme and biofilm production, the latter is forming through a number of mechanisms. Bacterial protease are enzymes help in break down other components of theenamel. Infection may then spread into the pulp of the tooth to form a pulp or root abscess, and then to the maxillary.