Protease production and characterization from actinomycetes BSU-9 strain

Proteases are obtained from a wide variety of sources such as plants, animals and microorganisms. In this thesis, the actinomycetes BSU-9 strain, producing protease, isolated from algae compost sample and was used. The actinomycetes BSU-9 strain was grown in broth medium and protease was characterized from supernatant. For the characterization of protease; optimum pH, optimum temperature, pH stability, temperature stability, and the effects of some inhibitors, metal ions, organic solvents, detergents, denaturants and hydrogen peroxide on protease activity were investigated. In addition, activity studies of the protease were performed by using zymogram. Extracellular protease was produced from BSU-9 strain. While this protease showed a wide stability in the range of pH 8-13, its optimum pH was determined as 11. It was found that the enzyme showed maximum activity at 65 ° C. While in the presence of EDTA, enzyme activity decreased by approximately 44 %, in the presence of PMSF, enzyme activity was largely inhibited. While the activity of the enzyme increased in the presence of MnCl2, it decreased in the presence of CuCl2. In the zymogram analysis of the protease, a single band is seen and the molecular weight of this band was determined to be approximately 45 kDa.