Purification and Biochemical Characterization of Phytase Enzyme from Lactobacillus brevis Isolated from Fresh Kashar Cheese

Abstract

In the last 20 years, phytase enzyme has attracted the attention of scientists in the fields of environmental protection, nutrition and biotechnology. Myo-inositol hexaphosphate phosphohydrolase (phytase), which is a type of phosphatase enzyme, catalyzes the hydrolysis of phytate into less phosphorylated inorganic phosphates and phytate. Phytases of microbial origin are widely used in biotechnological applications (paper industry, feed industry, food industry and soil improvement).
 In the present study, phytase enzyme was partially purified from Lactobacillus brevis NM-34 strain isolated from fresh kashar cheese and the pH and temperature values at which the enzyme showed optimum activity were determined. L. brevis NM-34 showed a phytase activity of 243.80 U/mL as a result of ammonium sulfate precipitation. In the ammonium sulfate range (40-60%), where the highest phytase activity was observed, the protein concentration was measured as 0.989 mg/mL. Km and Vmax values of phytase enzyme were determined as 0.0146 mM and 1.6 µmol/min, respectively. The pH and temperature values at which the partially purified phytase showed optimum activity were found to be pH 5 and 50 °C, respectively. Based on the findings from our research, the enzyme purified from this bacterium was found to have unique properties that make it suitable for use in industrial applications.