Isolation, purification and characterization of serine protease from medicinal plant Euphorbia prunifolia.

A new serine protease named “prunifoline” was purified from the latex of Euphorbia prunifolia, a medicinally important indigenous plant of Euphorbiacae family. “Prunifoline” was isolated using acetone precipitation method and purified by a sequence of DEAE cellulose column chromatography. The molecular weight of the purified protease was determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). “Prunifoline” a single protein band on SDS-PAGE and molecular weight was approximately 57.44 kDa. It remained active over a broad range of temperature but had optimum activity at 550C and pH 7.0 when casein was used as a substrate. Thus enzymes “prunifoline” may be considered as a strong candidate for various applications in the food and biotechnological industries.