Characterization of extracellular protease isolated from actinomycetes

In this study, characterization of extracellularly produced protease enzyme from Streptomyces sp. BSU-1 isolate was performed. Streptomyces sp. BSU-1 isolates were grown in glucose-containing medium for 3 days at 30 °C. The optimum reaction temperature and pH of the enzyme were found 60 °C and pH 10. It has been found that the protease enzyme maintains its activity over 80% at 50 C and pH 8-12 for 120 minutes. It was detected that Na+1, Ca+2, Zn+2 and Mg+2 retained the activity, Mn+2 and Cu+2 ions increased the activity, while Hg+2 metal ion decreased about 50%. When the effect of solvents on enzyme activity are examined, it is observed that activity is highly preserved. Tween-80 and Triton X-100 increased activity, while H2O2 caused loss of activity. The zymogram analysis of the enzyme showed single band and its molecular weight was found to be approximately 48 kDa