Abstract
Antisera raised in rabbits against native iodoacetamide- and iodoacetic acid-modified papain contained precipitating and non-inhibitory antibodies. Papain could be insolubilized as enzyme-antibody adducts with the gamma-globulin fraction derived from the antiserum. Two insolubilized papain preparations, designated A and B, with low and high antibody/enzyme ratios, respectively, exhibited high enzyme activity and markedly enhanced thermal and denaturant stabilities. However, papain antibody adduct B was superior in activity and stability over preparation A. The usefulness of immobilized papain in biopharmaceutical and other industries is also discussed.
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