PURIFICATION AND CHARACTERIZATION OF PAPAIN FROM CARICA PAPAYA LATEX: ITS APPLICATION IN THE HYDROLYSIS OF TIGERNUT PROTEIN HOMOGENATE

📄 Project Abstract

In this study, the production of tiger nut suspension was carried out using a proteolytic enzyme (papain) isolated from the latex of C. papaya. The crude papain isolated was subjected to three steps purification system of 80% ammonium sulphate saturation using sephadex G50 and G200 filtrations at pH 7.2 and 37oC. The protein concentration of the crude enzyme obtained was 136 g/ml, while its specific activity was 1.15U/mg. After 80% ammonium sulphate precipitation, the specific activity obtained was 1.31U/mg. Sephadex G50 and G200 filtrations gave specific activities of 1.48 and 1.28U/mg respectively. The optimal activity of papain was achieved at 90oC and pH 7.5 at 37oC and 1ml of 1% casein solution. The Vmax and Km were observed to be 1.133U/min/ml and 0.217g/min/ml respectively. Pure papain obtained was used to hydrolyse tiger nut protein at 37oC and pH 7.5 compared with O-pthalaldehyde as a standard hydrolysing agent. The degree of hydrolysis was monitored with tiger nut protein con...