Antidiabetic and immunomodulatory properties of peptide fractions from Sacha inchi oil press-cake
Sacha inchi (SI) oil press-cake (SIPC), a by-product of the sacha inchi oil extraction process, represents a novel protein source with potential bioactive applications in food. In this study, a sacha inchi protein concentrate (SPC) derived from SIPC was subjected to simulated gastrointestinal digest...
| Autores: | , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2025 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/385760 |
| Acceso en línea: | http://hdl.handle.net/10261/385760 |
| Access Level: | acceso abierto |
| Palabra clave: | Bioactive peptides Bioavailability Bioinformatics Molecular docking Plukenetia volubilis |
| Sumario: | Sacha inchi (SI) oil press-cake (SIPC), a by-product of the sacha inchi oil extraction process, represents a novel protein source with potential bioactive applications in food. In this study, a sacha inchi protein concentrate (SPC) derived from SIPC was subjected to simulated gastrointestinal digestion (SGID) using the INFOGEST 2.0 protocol. The resulting digests were fractionated by ultrafiltration (<3, 3–10, and >10 kDa), and the bioactive properties of the peptide fractions were evaluated. In vitro α-amylase inhibition was assessed, along with immunomodulatory markers (NO, IL-6, and TNF-α), in an ex vivo RAW 264.7 cell model. Both gastric and intestinal digests exhibited significant α-amylase inhibition (20–45%), with the <3 kDa intestinal fraction showing the highest inhibition (45% at 20 mg/mL). Both gastric and intestinal <3 kDa fractions reduced NO production in RAW 264.7 macrophages subjected to a lipopolysaccharide challenge. HPLC-MS/MS analysis facilitated de novo sequencing of the peptide fractions, identifying 416 peptides resistant to SGID through the find-pep-seq script, which were further assessed in silico for toxicity, allergenicity, and bioavailability, revealing no significant risks and potential drug-likeness development. Molecular docking simulations of three peptides (RHWLPR, RATVSLPR, and QLSNLEQSLSDAEQR) with α-amylase and four peptides (PSPSLVWR, RHWLPR, YNLPMLR, and SDTLFFAR) with the TLR4/MD-2 complex suggesting potential roles in α-amylase inhibition and anti-inflammatory activity, respectively. The findings suggest that SI protein concentrates could be used in functional foods to prevent starch breakdown through α-amylase-inhibiting peptides released during digestion, reduce blood glucose, and mitigate inflammation and oxidative tissue damage. |
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