Influence of dual succinylation and ultrasonication modification on the amino acid content, structural and functional properties of Chickpea (Cicer arietinum L.) protein concentrate.

Chickpea protein, a valuable plant-based source, offers versatile applications, yet the impact of modifications like succinylation and ultrasonication on its properties remains unclear. This study explored dual succinylation and ultrasonication modification to enhance its functionality and application. Modified chickpea protein with a degree of succinylation of 96.75 %, showed enhanced water holding capacity 39.83 %, oil holding capacity 54.02 %, solubility 7.20 %, and emulsifying capacity 23.17 %, compared to native protein. Despite reduced amino acid content (64.50 %), particularly lysine, succinylation increased sulfhydryl by 1.74 %, reducing hydrophobicity (Ho) by 41.87 % and causing structural changes. Ultrasonication further reduced particle size by 82.57 % and increased zeta potential and amino acid content (57.47 %). The dual-modified protein exhibited a non-significant increase in antimicrobial activity against Staphylococcus aureus (25.93 ± 1.36 mm) compared to the native protein (25.28 ± 1.05 mm). In conclusion, succinylation combined with ultrasonication offers a promising strategy to enhance chickpea protein's physicochemical properties for diverse applications.