Fractionation, Structural Characteristics, Functionality, Aromatic Profile, and In Vitro Digestibility of Lentil (<i>Lens culinaris</i>) Proteins
Liuyi Chang, Zixuan Gu, Nonoy Bandillo, Bingcan Chen, Jiajia Rao
Abstract
Consumers’ attitudes toward more plant-based components in their diet has greatly driven the exploration of functional plant proteins. The aim of this study was to systematically investigate the structural and functional properties, nutritional and aromatic profiles, and in vitro digestion of protein fractions from the underexploited lentil grain. Albumin (LA), globulin (LG), and its subunits legumin (LL) and vicilin (LV) were fractionated from red lentil flour through alkaline extraction–isoelectric precipitation and/or different salt extractions. LA and LV exhibited unique structural properties (more β-sheet and α-helix structures), higher solubility (almost 100% at pH 7.0), and foaming capacity (>200% at pH 7.0), while LG exhibited better emulsifying properties. LA showed a distinct aromatic profile including high numbers of volatile compounds, especially alcohols, esters, and acids. After in vitro gastric-intestinal digestion, the hydrolysis degree of LA (24.25%) was the lowest, owing to the presence of major antinutritional factors.