Chiang Mai Journal of Science

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Proteases from papaya peels were extracted with water followed by precipitation with ethanol and 57.6% yield was obtained. Their maximum hydrolysis of casein comparing to proteases from latex were similar in temperature but different in pH. Both of papaya proteases were fully activated by 5 mM cysteine, the peel enzymes were activated 1.6 times higher than latex enzymes. The peel proteases are also more stable in pH ≥ 8 and at 80oC than the latex proteases. Cathodic polyacrylamide gel electrophoresis and in situ proteolysis verified that papaya peel proteases are composed of papain as a major component, chymopapain, and possible two proteases which are absent in crude papain. Separation by anodic polyacrylamide gel electrophoresis and in situ proteolysis illustrated that proteases from papaya peels contained a protease with pI less than 8.3. Anion-exchange chromatography indicated that papaya peel proteases consisted of a number of proteins and proteases different from those found in papaya proteases.

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