Caricain

Caricain, historically referred to as Papaya peptidase A, is a highly basic cysteine protease isolated from the latex of the papaya plant (Carica papaya). It is a prominent member of the C1 family of peptidases (papain-like) and is one of the most abundant enzymes in papaya latex, alongside papain and chymopapain. Caricain is characterized by its broad proteolytic activity and a unique ability to efficiently cleave peptide bonds involving proline and glutamine residues. This specific activity makes it a valuable therapeutic agent for the degradation of immunogenic gluten peptides, which are responsible for triggering inflammatory immune responses in individuals with celiac disease. Beyond its role in digestive health, caricain is utilized in topical pharmaceutical preparations for the debridement of necrotic tissue in chronic wounds and ulcers. While it is used as a therapeutic enzyme (e.g., in the supplement GluteGuard), its application requires caution due to potential cross-reactivity in individuals with latex allergies and possible interactions with anticoagulant therapies.

Other names

CaricainPapaya peptidase IIPapaya proteinase IIIPapaya proteinase omegaProteinase omegaPapaya proteinase AChymopapain S

Enzymatic hydrolysis of peptide bonds; specifically targets and neutralizes immunogenic proline- and glutamine-rich sequences in gluten to prevent the activation of T-cells in the intestinal mucosa.