How Can Tarwi Turn Into a Super‑Ingredient for Health?

Tarwi, or Lupinus mutabilis, is an Andean legume packed with protein that is gaining attention in the functional food arena. Researchers isolated its albumin protein fraction using tangential ultrafiltration, then broke it down with a natural protease, PC7, produced by a Micrococcus bacterium. After fine‑tuning the enzyme‑to‑substrate ratio and reaction times, they created two hydrolysates: HAP (PC7 only) and HAPA (PC7 followed by alcalase).

In‑vitro tests showed both hydrolysates can neutralize free radicals, thanks to antioxidant activity measured with ABTS and ORAC assays. They also inhibit ACE, an enzyme that controls blood pressure, and DPP‑IV, involved in glucose metabolism. These traits suggest tarwi‑derived peptides could help manage oxidative stress, hypertension, and metabolic disorders, though they are not a replacement for medication or medical diets.

The outcome is a multifunctional ingredient ready for inclusion in bars, drinks, or snacks for those who want to look after their bodies naturally. The next step will be safety and efficacy trials in humans, but tarwi already stands out as a promising resource for the future of nutrition.

The proteomic analysis of Lupinus mutabilis albumin was performed with OmicsBox, classifying proteins into three functional categories: cellular components (35.57 %), molecular functions (33.45 %) and biological processes (30.97 %). The albumin fraction, rich in globulins and albumins, is especially suitable for generating bioactive peptides due to its flexible structure and the presence of sequences abundant in hydrophobic and aromatic amino acids, known to confer antioxidant activity.

The PC7 protease, belonging to the serine protease family, exhibits cleavage specificity that favors the release of peptide sequences 2‑12 residues long, an optimal size for intestinal absorption. Optimizing the enzyme‑to‑substrate ratio (E/S) at 1:50 (w/w) and incubation time to 2 h maximized the degree of hydrolysis (DH) around 25 %, balancing active peptide production with solubility preservation.

A subsequent step with alcalase further increased DH to about 35 %, generating a more heterogeneous peptide mixture (HAPA). Antioxidant activities measured with ABTS (IC50 ≈ 0.45 mg mL⁻¹) and ORAC (≈ 1.2 mmol TE g⁻¹) indicate scavenging capacity comparable to green‑tea extracts. Inhibition of ACE (IC50 ≈ 0.30 mg mL⁻¹) and DPP‑IV (IC50 ≈ 0.25 mg mL⁻¹) suggests the peptides contain sequences similar to those of antihypertensive drugs (e.g., lysine‑proline) and GLP‑1 modulators.

Molecular docking studies revealed hydrogen bonds and hydrophobic interactions between the peptides and the active sites of ACE and DPP‑IV, confirming the plausibility of competitive inhibition. Nevertheless, gastrointestinal stability of the peptides remains to be assessed: simulated gastric tests showed a 20 % degradation after 30 min, indicating the need for protective formulations (e.g., microencapsulation). In summary, L. mutabilis albumin is a rich source of multifunctional peptides with potential use in functional foods targeting oxidative stress and metabolic dysfunctions.