ArticleJournal of food science2026
Papain- and Trypsin-Derived Spirulina Peptides: Antiproliferative and Antioxidant Profiles.
Article in Journal of food science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Enzymatic hydrolysis can release bioactive peptides from spirulina proteins, but the influence of protease type and molecular-weight fraction on antioxidant and cell viability endpoints remains incompletely defined. This study compared papain- and trypsin-derived fractions from a food-grade, C-phycocyanin-rich spirulina preparation. Hydrolysis was monitored by UV‒visible spectroscopy and quantified using the o-phthaldialdehyde degree-of-hydrolysis assay, after which six membrane-derived fractions (P1, P5, P10, T1, T5, and T10) were evaluated by ferric-reducing antioxidant power (FRAP) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical-scavenging assays. Fractions below 5 kDa (P1, P5, T1, and T5) were additionally screened in MCF-7 estrogen receptor-positive breast adenocarcinoma cells, a widely used model for preliminary assessment of food-derived antiproliferative activity, and in MCF-10A nontumorigenic breast epithelial cells. Papain at pH 6.5 produced the highest measured degree of hydrolysis (21.4 ± 1.8%). At 500 µg/mL for 48 h, P1, P5, T1, and T5 reduced MCF-7 metabolic viability to 20.83 ± 4.33%, 28.43 ± 4.32%, 21.14 ± 4.33%, and 29.00 ± 4.95%, respectively. Screening-level IC
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