Ficin

Ficin is a sulfhydryl cysteine protease enzyme extracted primarily from fig latex (Ficus species, including Ficus carica, Ficus glabrata). As a purified enzyme preparation, it does not function as a conventional nutritional ingredient with meaningful macronutrient or micronutrient contributions at typical use concentrations. Key biochemical composition: Ficin is a glycoprotein with a molecular weight of approximately 23,800–26,000 Da; it contains a catalytic cysteine residue essential for proteolytic activity. The enzyme is typically supplied as a partially purified latex extract or lyophilized powder with protease activity measured in units (e.g., units/mg protein). Protein content of crude fig latex preparations ranges broadly depending on purification grade, with ficin representing a significant fraction of total soluble protein in latex. Bioactive compounds: The primary bioactive is the ficin enzyme itself, with proteolytic specificity toward fibrinogen, elastin, collagen, and casein substrates. Fig latex also contains minor cysteine proteases (ficin isoforms A, B, C, D), peroxidases, and polyphenols in crude extracts, though these are largely removed in pharmaceutical-grade preparations. Carbohydrate content: Ficin contains approximately 5–10% covalently linked carbohydrate (mannose and N-acetylglucosamine residues) as part of its glycoprotein structure. Bioavailability: As a protein enzyme, oral ficin is subject to degradation by gastric acid and pepsin, substantially limiting systemic bioavailability; enteric coating or co-formulation strategies are typically required for any intended systemic proteolytic effect. Ophthalmic or injectable preparations bypass this limitation entirely.