Comparison of Pyruvate Kinase of different species of Lactic Acid Bacteria

Abstract

Pyruvate kinase (PK) is an important allosterically regulated enzyme that connects Glycolysis from the primary energy to cellular metabolism. It catalyzes the last step of Glycolysis by producing one mole of energy in the form of ATP. On the other hand, Lactic acid bacteria (LAB) under anaerobic condition produce energy by Glycolysis process that strengthens the vital role of PK in their cellular metabolism. The recombinant proteins of PKs expression were performed by inserting the PKs genes of LAB strains in the pET 30 plasmid and transformed into the E. coli BL21 (DE3) cells. After cell cultivation, recombinant protein expression was induced. The targeted protein was purified by Affinity chromatography and quantified by Bradford quantitative assay. Protein expression was compared by the SDS-PAGE. Here in this study, the main targeted protein is Pyruvate kinase and its activity is compared among Enterococcus faecalis, Lactococcus lactis, Lactococcus plantarum and Streptococcus pyogenes.