Purification and analysis of the properties of the prosthese enzymes from bacillus subtilis megatherium bacteria

Enzymes are biocatalysts produced by living organisms that affect the working speed of important biological reactions. Enzyme technology is developing rapidly today and is gaining importance due to the diversity of products and economic values. The most important enzyme used in this field is protease. Proteases are used very frequently in the detergent, food, pharmaceutical and leather industries. More than 60% of the enzymes are sourced from microorganisms. The aim of our study is to purify the protease enzyme from Bacillus subtilis megatherium bacteria and to determine its properties. In the first step of the study, the production of the enzyme was provided under suitable conditions. For purification, dialysis, precipitation with ammonium sulfate and DEAE-Sepharose ion exchange chromatography methods were performed. The crude homogenate specific activity was found 10.2 U / mg after the procedures. After 80% precipitation, the solution specific activity was 12.9 U / mg. 1.2 times purification was achieved after saturation. Protease enzyme's optimum temperature, temperature stability, optimum pH and pH stability; the inhibitory and activator effects on the reaction, the duration of the reaction and the effect of the substrate were examined and molecular weight was determined.