STUDI AKTIVITAS ENZIM PROTEASE EKSTRASELULER STREPTOKOKUS GRUP B (Streptococcus agalactiae) PADA SUBSTRAT MUSIN
Abstract
Group B Streptococci (GBS) produce extracellular enzymes which are know to be involved in
virulence mechanism. One of the enzymes is protease which has an ability to degradate mucin. Mucin has
an important role to defend mucosal membrane from invasion of bacteria. The purpose of this research
was to analysis protease characteristics of GBS on the mucin substrat as a model for studying the role of
GBS proteases in pathogenesis of GBS infections. The optimum pH for the enzym was 7 and the enzyme
had maximal activity at 370 C. The protease activity was inhibited by EDTA (2 mM and 5 mM) and PMSF
(2 mM and 5 mM). The protease activity was enhanced by addition of MgCl2, CaCl2, and Fe2Cl3 (2 mM
and 5 mM).
virulence mechanism. One of the enzymes is protease which has an ability to degradate mucin. Mucin has
an important role to defend mucosal membrane from invasion of bacteria. The purpose of this research
was to analysis protease characteristics of GBS on the mucin substrat as a model for studying the role of
GBS proteases in pathogenesis of GBS infections. The optimum pH for the enzym was 7 and the enzyme
had maximal activity at 370 C. The protease activity was inhibited by EDTA (2 mM and 5 mM) and PMSF
(2 mM and 5 mM). The protease activity was enhanced by addition of MgCl2, CaCl2, and Fe2Cl3 (2 mM
and 5 mM).
Keywords
protease, SGB, mucin, enzym characterization, purification.