Cysteine protease (capparin) from capsules of caper (Capparis spinosa)

Proteases are enzymes that perform very important functions in organisms and are used for a variety of objectives in vitro. In recent years, proteases have been used for clinical, pharmaceutical (alimentary digestion, anti-inflammatory, etc.) and industrial applications (cheese production, meat tenderizing, leather tanning). In this research, a protease has been purified from capsules of caper (Capparis spinosa) and characterized. Caper plants have been used for food and medicine since ancient times. The plant grows abundantly in certain regions of Turkey. Ammonium sulphate fractionation and a CM Sephadex column were used for purification of the enzyme. The purification enzyme has an optimum pH=5.0 and its optimum temperature was 60 degrees C. The nu(max) and K-m values determined by Lineweaver-Burk graphics were 1.38 mu g/(L.min) and 0.88 mu g/L, respectively. The purification degree and the molecular mass of the enzyme (46 kDa) were determined by SDS-PAGE and gel filtration chromatography. It was investigated whether the purified and characterized protease could cause milk to congeal or digest chicken and cow meat. The results show that protease can be used for industrial production.