Insights into amino acid usage patterns among allergenic and non‐allergenic proteins to develop biomarkers for early detection of food‐allergenic proteins

BACKGROUND Millions of people face severe health challenges because of food allergy reactions to proteins known as food allergens that can trigger allergic reactions when ingested. Understanding their structure and function is essential for early detection and risk assessment. RESULTS These findings suggest distinct differences in amino acid compositions, conserved motifs, and solubility profiles, which enhances the understanding of allergenicity and protein functionality. Correspondence analysis was utilized to differentiate between allergenic and non‐allergenic proteins based on relative amino acid usage data derived from CodonW. A correspondence analysis biplot differentiated between allergenic and non‐allergenic proteins. Certain amino acids were found to be significantly overrepresented in the chi‐square (χ 2 ) test for allergenic protein families, with a significance level of P < 0.05. Additionally, some conserved motifs exhibited a 70% identity level among the allergenic proteins of the Cupin, Bet v 1‐homologous, CAP (cysteine‐rich secretory protein), and Tropomyosin families. A solubility analysis showed that allergenic Bet v 1‐homologous proteins are more soluble than non‐allergenic proteins. In contrast, Cupin, CAP, and Tropomyosin allergens are less soluble than their non‐allergenic counterparts. CONCLUSION This study aims to examine the amino acid usage patterns of allergenic and non‐allergenic proteins to identify features that make certain proteins allergenic. The results revealed clear differences in amino acid composition, conserved motifs, and solubility between allergenic and non‐allergenic proteins. Overall, these findings improve our understanding of the structural and physicochemical traits that contribute to allergenicity and provide a basis for developing biomarkers for early detection of food allergens.