2026-04-04T17:11:00Z https://meral.edu.mm/oai

oai:meral.edu.mm:recid/00007110 2022-03-24T23:13:04Z 1607925118212 1607925118212:1608025613610 user-mub

Enzymatic Studies on Crude Papain from Papaya Peels Nwe Mar Lin Khin Sandar Linn Yee Mun Than Myat Kyaw Thu Papain (EC 3.4.22.2) is the most important plant proteolytic enzyme present in the latex, leaves, roots and fruits of the papaya plants. In this research, partially purified papain enzyme was isolated from matured green papaya peels by ammonium sulphate precipitation (20 % - 70 %) method. The partially purified papain was qualitatively examined by skim milk powdered test for its milk clotting activity. Papain activity was determined by spectrophotometric method using tyrosine as standard and casein as substrate at 273 nm. Protein content was determined by Biuret method using Bovine Serum Albumin (BSA) as standard at 560 nm. Specific activities, protein recovery and degree of purification were determined in each purification steps. Papain was purified 8.6 fold over crude extract and protein recovery was found to be 31.50 %. Specific activity of papain in crude extract was 0.0045 μmol min-1 mg-1 and increased to 0.0387 μmol min-1 mg-1 after 70 % ammonium sulphate precipitation. The optimum pH of the papain - catalyzed reaction was determined by using different pH values (6 - 8) and the maximum papain activity was found at 7.4. The optimum temperature of the papain - catalyzed reaction was conducted at different temperature in the range of (27􀎹C - 87 􀎹C) and the highest papain activity was observed at 67 􀎹C. 2020-12-01 http://hdl.handle.net/20.500.12678/0000007110 https://meral.edu.mm/records/7110