This is an abbreviated version, for detailed information about chymopapain, go to the full flat file.
Similar to that of papain
Chymopapain, chymopapain A, chymopapain B, chymopapain isoform II, chymopapain isoform III, chymopapain isoform IV, Chymopapain S, EC 184.108.40.206, More, papaya proteinase II, PPII
pH Stability on EC 220.127.116.11 - chymopapain
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at low pH, the enzyme undergoes a conformational transition that instantaneously converts their native form into molten globule that are quite unstable and rapidly degraded by pepsin. The denatured state of these proteinase which results from acid treatment is completely irreversible
protein unfolds following biphasic kinetics. Two different effects of electrolyte concentration on unfolding reaction are observed. At low ionic strength, the ionic atmosphere causes an increase in reaction rates, regardless of the type of ions being present. This effect is attributed to a general electrostatic screening of charge-charge interactions in the macromolecule. At high ionic strength, each electrolyte exerts a distinctly different effect: both rate constants are largely increased by guanidinium-HCl but slightly by LiCl. Na2SO4 decreases the value of both unfolding rates
2 - 3
enzyme undergoes conformational transition that instantaneously converts the native form into a molten globule state and is completely irreversible