Purification of phytase enzyme from Lactobacillus brevis and biochemical properties

In this study, Lactobacillus brevis isolated from kashar cheese was identified by 16s rRNA method, phytase enzyme from bacteria was partially purified and characterized. Work continued in two directions. The first step was the isolation and identification of the bacteria. In the second step, the phytase enzyme from L. brevis was partially purified and the optimum pH and temperature values of the purified enzyme were determined. The phytase activity of the identified L. brevis was determined as 212.97 U/mL. The molecular mass of the enzyme was determined as 49.9 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) method. The K m and V max values for sodium phytate were 0.0154 mM and 2.00 µmol/min, respectively. The optimum pH and temperature values of partially purified phytase were determined as pH 3.0, 60 °C, respectively.