Allergenicity profiling of Sesamum indicum seed proteins

This study aimed to isolate, purify, and identify allergenic proteins present in Sesamum indicum seeds. Proteins were extracted using isoelectric precipitation, yielding a high-purity product with a protein content of 96.7%. The extracted allergens were further characterized using SDS-PAGE, HPLC, immunoblotting, and proteomic analysis for amino acid sequence identification. SDS-PAGE analysis revealed that the molecular weights of the reduced protein fractions ranged from approximately 15 to 50 KDa. The purified allergens exhibited strong IgE-binding inhibition, reducing IgE interaction with crude seed extract by up to 90%. Tryptic peptide analysis identified conserved sequences such as AIFALPQAKIA in black sesame and VQLAIHTLKSG—both homologous to known legumin peptides from garden pea. Overall, the majority of sesame seed proteins were classified as minor allergens, exhibiting low prevalence and limited allergenic potency.

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Publication Details

Journal
International Journal of Applied Research
Published
2025-01-01
DOI
https://doi.org/10.22271/allresearch.2025.v11.i8d.12808
Primary Topic
Sesame and Sesamin Research
Type
article
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article

Allergenicity profiling of Sesamum indicum seed proteins

Sohana Reddy Samala, Praveen Kumar Vemuri, S. A. Basha, Mythri Nandhala et al.
International Journal of Applied Research
Sesame and Sesamin Research
article

Allergenicity profiling of Sesamum indicum seed proteins

Sohana Reddy Samala, Praveen Kumar Vemuri, S. A. Basha, Mythri Nandhala, Rishitha Golla, Veda Naga Sai Rithika Pilli, UM Siva Ramakrishna Polnati
article en

Abstract

This study aimed to isolate, purify, and identify allergenic proteins present in Sesamum indicum seeds. Proteins were extracted using isoelectric precipitation, yielding a high-purity product with a protein content of 96.7%. The extracted allergens were further characterized using SDS-PAGE, HPLC, immunoblotting, and proteomic analysis for amino acid sequence identification. SDS-PAGE analysis revealed that the molecular weights of the reduced protein fractions ranged from approximately 15 to 50 KDa. The purified allergens exhibited strong IgE-binding inhibition, reducing IgE interaction with crude seed extract by up to 90%. Tryptic peptide analysis identified conserved sequences such as AIFALPQAKIA in black sesame and VQLAIHTLKSG—both homologous to known legumin peptides from garden pea. Overall, the majority of sesame seed proteins were classified as minor allergens, exhibiting low prevalence and limited allergenic potency.

International Journal of Applied ResearchVol. 11(8)
Ramakrishna Mission Vidyamandira (IN), University of Hyderabad (IN), Andhra Pradesh Forest Department (IN), Science Health Allied Research Education (IN)
Zero hunger
Openalex Percentile: Top 84%
Sesame and Sesamin Research
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