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 Structure

The three-dimensional structures of all papaya proteinases are very similar to that of papain "stricto sensu". The elements of secondary structure, the conformation around the active site, and the asymmetrical environment of the aromatic residue, were found to be almost identical.

The secondary structure in combination with the presence of four disulfide bonds and a multitude of hydrogen-hydrophobic and electrostatic interactions makes these proteolytic enzymes particularly resistant to denaturation by heat and chaotropic solvents.

For reasons not yet fully understood, the chymopapain fraction is much more resistant to acid denaturation than the three other proteinases. This makes the refined papain from ENZYMASE efficient in wide range of pH.



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