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Dietary Bioactive Components (Poster Session)

(P04-006-24) In Vitro Antidiabetic Potential Chia Seed (Salvia hispanica L.) Co-product Protein Fractions and Hydrolysates

Sunday, June 30, 2024
12:45 PM – 1:45 PM CT
Location: Poster Board 83

    Presenting Author(s)

  • GB

    Gislane Briceño-Islas, MSc. (she/her/hers)

    PhD Candidate
    Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C.
    Zapopan, Jalisco, Mexico

    • Co-Author(s)

  • JU

    Judith Esmeralda Urías-Silvas

    Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C.
    Zapopan, Jalisco, Mexico

  • LM

    Luis Mojica

    Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C., Mexico

Disclosure(s):
Gislane Briceño-Islas, MSc.: No relevant financial relationship(s) with ineligible companies to disclose.


Objectives: This work aimed to evaluate the antidiabetic potential of chia seed protein hydrolysate and ultrafiltrates of 30, 10, and 3 kDa using in vitro tools.

Methods: The chia cake (co-product of oil extraction) was subjected to isoelectric precipitation, thus obtaining the protein isolate. The isolate was characterized biochemically, the soluble protein content was evaluated using the Bradford method, and its electrophoretic profile was assessed using SDS-PAGE electrophoresis. Enzymatic hydrolysis was carried out with thermolysin from Geobacillus stearothermophilus (HT), and the degree of hydrolysis was quantified. The hydrolysate was ultrafiltered with membranes of 30 (P30), 10 (P10), and 3 (P3) kDa, where the permeate was obtained. The Lowry method quantified HT, P30, P10, and P3 soluble protein, and the electrophoretic profile was carried out on Tricine SDS-PAGE gels. The antidiabetic activity was evaluated by inhibiting α-amylase, α-glucosidase, and dipeptidyl peptidase IV (DPP-IV) in vitro.

Results: The chia cake isolate had 78% protein, and 50, 30, and 20 kDa bands were observed in its electrophoretic profile. The degree of hydrolysis of HT was 13.6%. Regarding the electrophoretic profile in HT and P30, bands between 14 and 3 kDa predominated. In P10, bands smaller than 6 kDa were observed, and in P3, bands smaller than 3 kDa were observed. HT's showed higher inhibition for α-amylase, α-glucosidase, and DPP-IV compared to the ultrafiltrates (p < 0.05). The IC50 of HT was 1.76 mg/mL, 0.42 mg/mL, and 0.46 mg/mL, respectively.

Conclusions: Chia co-product protein hydrolysates inhibited important therapeutic targets in the treatment of type 2 diabetes. The co-product of the chia seed industry is a promising source of peptides with antidiabetic potential and could be used in de development of functional foods.

Funding Sources: The author was supported by a scholarship from CONAHCYT-México (CVU: 896150) and Proyecto Ciencia de Frontera 2023-CONAHCYT, CF-2023-I-2694.