Pea albumin, glutelin and globulin interactions with curcumin and their effects on in vitro gastric digestibility

Tuesday, April 30, 2024

5:00 PM – 6:00 PM EDT

Presenting Author(s)

Judith O. Oballa, B.Tech Biology (she/her/hers)

Graduate Student (MSC)
University of Ottawa
Ottawa, ON, Canada

Co-Author(s)

Chibuike Udenigwe, PhD

Full Professor & University Research Chair
University of Ottawa, Ontario, Canada

Abstract: Pea (Pisum sativum) is considered a source of high-quality protein. In this study, three pea protein fractions, including albumin, globulin, and glutelin, were investigated for their interaction with curcumin, and the resulting effect on physicochemical properties and in vitro protein digestibility in the gastric phase. Mixing the protein fractions (0.25 mg/mL) with curcumin (2-100 μM) decreased the average particle size based on dynamic light scattering. Ultraviolet-visible spectroscopy, which showed decreased transmittance, and surface hydrophobicity analysis revealed the formation of protein-curcumin complexes. . Transmission electron microscopy revealed the formation of nanocomplexes for albumin and globulin fractions and ordered sheet-like structures for glutelin fraction after complex formation. Curcumin binding did not alter the protein profiles, as demonstrated by reducing SDS-PAGE. Furthermore, curcumin binding significantly decreased the degree of hydrolysis of albumin, globulin and glutelin by 76.64%, 58.67%, and 0%, respectively, indicating that the resulting protein aggregation may have hindered pepsin accessibility to the proteins for hydrolysis. The results reflect the possible effect of the binding on protein digestibility at the intestinal phase and undigested peptide fractions in the colon. The study enhances the understanding of how interactions between food biomolecules influence the nutritional value of protein in food products and dietary supplements.