Cottonseed Vicilin Proteins: Potential Allergen Risk and Source of Bioactive Peptides

Glandless cottonseed (Glc) is an exciting new food source but contains C72 and GC72A vicilin proteins similar to the Ara h 1 peanut allergen. The objective here was to evaluate some of the immunologic, catabolic, and bioactive peptide properties of the C72 and GC72A proteins. Immunoblot assay indicated that C72 and GC72A were recognized by three anti-Ara h 1 antibodies. Enzyme-linked immunosorbent assay (ELISA) with purified native C72 and GC72A showed they were recognized by IgE from 13 of 25 (∼50%) peanut or tree-nut-allergic sera. A subset of these sera also recognized recombinant C72 and GC72A. In vitro simulated digestion indicated that Glc proteins were readily digested. In silico analysis revealed that C72, GC72A, and other cupin domains containing Glc proteins are potential sources of bioactive peptides. The results presented here indicate that the C72 and GC72A proteins represent an allergen concern and potential source of bioactive peptides in food applications.

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Publication Details

Journal
ACS Food Science & Technology
Published
2025-01-27
DOI
https://doi.org/10.1021/acsfoodscitech.4c00577
Citations
4
Primary Topic
Transgenic Plants and Applications
Type
article
Field-Weighted Citation Impact
4.93

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Cottonseed Vicilin Proteins: Potential Allergen Risk and Source of Bioactive Peptides

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ACS Food Science & Technology
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article

Cottonseed Vicilin Proteins: Potential Allergen Risk and Source of Bioactive Peptides

Zhongqi He, Małgorzata Darewicz, Piotr Mińkiewicz, Rebecca A. Dupre, Christopher P. Mattison, Tien Thuy Vuong
article en
4 citations

Abstract

Glandless cottonseed (Glc) is an exciting new food source but contains C72 and GC72A vicilin proteins similar to the Ara h 1 peanut allergen. The objective here was to evaluate some of the immunologic, catabolic, and bioactive peptide properties of the C72 and GC72A proteins. Immunoblot assay indicated that C72 and GC72A were recognized by three anti-Ara h 1 antibodies. Enzyme-linked immunosorbent assay (ELISA) with purified native C72 and GC72A showed they were recognized by IgE from 13 of 25 (∼50%) peanut or tree-nut-allergic sera. A subset of these sera also recognized recombinant C72 and GC72A. In vitro simulated digestion indicated that Glc proteins were readily digested. In silico analysis revealed that C72, GC72A, and other cupin domains containing Glc proteins are potential sources of bioactive peptides. The results presented here indicate that the C72 and GC72A proteins represent an allergen concern and potential source of bioactive peptides in food applications.

ACS Food Science & TechnologyVol. 5(2)
Southern Regional Research Center (US), University of Warmia and Mazury in Olsztyn (PL)
Ministerstwo Edukacji i Nauki, Agricultural Research Service
Zero hunger
Openalex Percentile: Top 6%
Transgenic Plants and Applications
4.93
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