Exploring the Amino-Acid Composition, Secondary Structure, and Physicochemical and Functional Properties of Chickpea Protein Isolates

[Image: see text] This study examined the amino-acid profile, secondary structure, and physicochemical and functional properties of proteins isolated from Anatolian chickpea landraces. Secondary objective of the study was to determine whether a relationship exists between the amino-acid composition and physicochemical and functional properties. Aspartic acid and glutamic acid were the dominant amino acids, while the isolates were deficient in methionine. Secondary structures were determined by Fourier transform infrared spectroscopy, where the β-sheet was shown to be dominant. The denaturation temperature of the isolates was between 87 and 145 °C, and the highest net surface charge (≃28.6 mV) and solubility (∼95.0%) were observed at pH 9.0–10.0. The isolates’ water-holding capacity varied between 2.1 and 2.7 g water/g protein, whereas their oil-holding capacity ranged between 3.4 and 4.4 g oil/g protein. Emulsion capacity, emulsifying activity, and the stability indices of isolates were found to be between 401.2 and 469.1 g oil/g protein, 14.5 and 25.7 m(2)/g, and 45.7 and 146.9 min, respectively. Isolates of Hisar and Erzincan chickpeas exhibited good emulsifying properties. The Yasa isolate had a relatively high hydrophobic amino-acid content and delivered the best gelation performance. Overall, significant differences in the characteristics of proteins were observed among the different chickpea landraces studied.