Identification and characterization of proteases from Tabernaemontana divaricata

Abstract

During the screening of latex collected from several native plant sources, good protease activity was observed in the latex of Tabernaemontana divericata (Apocynaceae). The proteases from the latex of T. divaricata were characterized by studying the effect of temperature, pH, latex volume, substrate volume and time kinetics. The stability of the protease activity was also studied. Native polyacrylamide gel electrophoresis and substrate polyacrylamide gel electrophoresis were performed to analyze the proteases in the latex sample. From the results, the optimum protease activity was observed at pH 5.0 and 50°C temperature. Enzyme activity was lost over a period of 5 days at room temperature, whereas the enzyme activity was relatively stable at 0°C. Three types of protease molecules were found in the latex of T. divaricata, whose molecular weights were 54.95 kDa, 21.87 kDa and 20.89 kDa. Proteases are important molecules in the living organisms as they carry out crucial biological functions including immunity. Apart from their biological functions, proteases play important role in a variety of industrial applications such as- an additive in detergents, food processing, brewing and leather tanning. online