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Enzymatic Studies on Crude Papain from Papaya Peels

http://hdl.handle.net/20.500.12678/0000007110
ad4f4634-3f10-4fe4-a6d4-fc799e491d0f
1ea368ab-a88e-4167-a91e-a569183bab0b
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5 5 Nwe Mar Lin, Khin Sandar Linn.pdf (275 KB)
Publication type
Journal article
Upload type
Publication
Title
Title Enzymatic Studies on Crude Papain from Papaya Peels
Language en
Publication date 2020-12-01
Authors
Nwe Mar Lin
Khin Sandar Linn
Yee Mun Than
Myat Kyaw Thu
Description
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.
Keywords
Papain, Papaya peels, Ammonium sulphate precipitation method, Milk clotting activity, Spectrophotometric method
Journal articles
Maubin University Research Journal
p. 173-180
Vol.11
1383
1492
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