Comparative Assessment of Albumins from Ten Pulses: Technofunctional Properties and Amino Acid Profiles for Sustainable Food Applications

Abstract

Pulse albumins—often recovered as by-products from pulse processing—are gaining increasing attention. This study compared the techno-functional properties and amino acid profiles of albumins extracted from ten pulses, including Vigna radiata (mung bean, MB), Vigna angularis (adzuki bean, RB), Phaseolus vulgaris (red kidney bean, RK; white kidney bean, WK), Cicer arietinum (kabuli chickpea, KCP; desi chickpea, DCP), Pisum sativum (green pea, GP; yellow pea, YP), Vicia faba (broad bean, BB), and Lens culinaris (lentil, LP). All assayed albumins exhibited excellent solubility (>70%) across a broad pH range (3–9), demonstrating pH-independent behavior. Notable interspecies variations were observed: P. vulgaris albumins (WK, RK) retained high solubility (>76%) even at 10% (w/v) protein concentration, while P. sativum albumins (GP, YP) showed outstanding foaming capacity and stability. Compared to whey protein (WP), most pulse albumins exhibited superior foam formation and stability but lower emulsifying activity, emulsion stability, and oil-holding capacity. Notably, P. vulgaris(RK, WK) and P. sativum (YP), displayed higher water-holding capacity than WP. Amino acid analysis revealed that pulse albumins are rich in negatively charged residues, contributing to their high solubility. All samples showed lysine scores above 100 and essential-to-total amino acid (E/T) ratios exceeding FAO/WHO standards. Furthermore, P. vulgaris (RK, WK) and P. sativum (GP) albumins exhibited strong sulfur-containing amino acid profiles (AAS >100), with P. vulgaris (WK, RK) also displaying the highest essential amino acid index (EAAI), biological value (BV), and branched-chain amino acid content.