{"created":"2020-12-30T09:31:11.705032+00:00","id":7110,"links":{},"metadata":{"_buckets":{"deposit":"1ea368ab-a88e-4167-a91e-a569183bab0b"},"_deposit":{"created_by":153,"id":"7110","owner":"153","owners":[153],"owners_ext":{"displayname":"","email":"tunhtethtetaung@gmail.com","username":""},"pid":{"revision_id":0,"type":"depid","value":"7110"},"status":"published"},"_oai":{"id":"oai:meral.edu.mm:recid/00007110","sets":["1607925118212","1607925118212:1608025613610"]},"communities":["mub"],"item_1583103067471":{"attribute_name":"Title","attribute_value_mlt":[{"subitem_1551255647225":"Enzymatic Studies on Crude Papain from Papaya Peels","subitem_1551255648112":"en"}]},"item_1583103085720":{"attribute_name":"Description","attribute_value_mlt":[{"interim":"Papain (EC 3.4.22.2) is the most important plant proteolytic enzyme present in the latex, leaves, roots\nand fruits of the papaya plants. In this research, partially purified papain enzyme was isolated from\nmatured green papaya peels by ammonium sulphate precipitation (20 % - 70 %) method. The partially\npurified papain was qualitatively examined by skim milk powdered test for its milk clotting activity.\nPapain 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\n(BSA) as standard at 560 nm. Specific activities, protein recovery and degree of purification were\ndetermined in each purification steps. Papain was purified 8.6 fold over crude extract and protein\nrecovery was found to be 31.50 %. Specific activity of papain in crude extract was 0.0045 μmol min-1\nmg-1 and increased to 0.0387 μmol min-1 mg-1 after 70 % ammonium sulphate precipitation. The\noptimum pH of the papain - catalyzed reaction was determined by using different pH values (6 - 8) and\nthe maximum papain activity was found at 7.4. The optimum temperature of the papain - catalyzed\nreaction was conducted at different temperature in the range of (27􀎹C - 87 􀎹C) and the highest papain\nactivity was observed at 67 􀎹C."}]},"item_1583103108160":{"attribute_name":"Keywords","attribute_value_mlt":[{"interim":"Papain"},{"interim":"Papaya peels"},{"interim":"Ammonium sulphate precipitation method"},{"interim":"Milk clotting activity"},{"interim":"Spectrophotometric method"}]},"item_1583103120197":{"attribute_name":"Files","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_access","date":[{"dateType":"Available","dateValue":"2020-12-30"}],"displaytype":"preview","filename":"5 Nwe Mar Lin, Khin Sandar Linn.pdf","filesize":[{"value":"275 KB"}],"format":"application/pdf","licensetype":"license_0","url":{"url":"https://meral.edu.mm/record/7110/files/5 Nwe Mar Lin, Khin Sandar Linn.pdf"},"version_id":"e7986c17-3964-446a-96b8-61a15b8ee957"}]},"item_1583103131163":{"attribute_name":"Journal articles","attribute_value_mlt":[{"subitem_journal_title":"Maubin University Research Journal","subitem_pages":"p. 173-180","subitem_volume":"Vol.11"}]},"item_1583105942107":{"attribute_name":"Authors","attribute_value_mlt":[{"subitem_authors":[{"subitem_authors_fullname":"Nwe Mar Lin"},{"subitem_authors_fullname":"Khin Sandar Linn"},{"subitem_authors_fullname":"Yee Mun Than"},{"subitem_authors_fullname":"Myat Kyaw Thu"}]}]},"item_1583108359239":{"attribute_name":"Upload type","attribute_value_mlt":[{"interim":"Publication"}]},"item_1583108428133":{"attribute_name":"Publication type","attribute_value_mlt":[{"interim":"Journal article"}]},"item_1583159729339":{"attribute_name":"Publication date","attribute_value":"2020-12-01"},"item_title":"Enzymatic Studies on Crude Papain from Papaya Peels","item_type_id":"21","owner":"153","path":["1607925118212","1608025613610"],"publish_date":"2020-12-30","publish_status":"0","recid":"7110","relation_version_is_last":true,"title":["Enzymatic Studies on Crude Papain from Papaya Peels"],"weko_creator_id":"153","weko_shared_id":-1},"updated":"2022-03-24T23:13:04.266630+00:00"}