Abstract
This study aimed to improve lentil proteins' (LPs) functionality and nutritional value, specifically addressing their lower water solubility and digestibility. A unique combination of LP-disaccharide interactions was employed. Spectroscopic technologies, which include fluorescence spectra, ultraviolet spectra, and Fourier-transform infrared, investigated the structure of LPs at various concentrations of trehalose. The results indicate that the LP structures and conformation were considerably modified (p < 0.05) following trehalose conjugation. The surface charge and hydrophobicity of the trehalose-conjugated LPs (T-LPs) were significantly altered (p < 0.05), from -22.7 to -31.4 and 753 and 543 a.u., respectively. Furthermore, the digestibility and solubility of T-LPs increased from 75% to 81.8% and 60% to 66%, respectively. In conclusion, this study showed that combining LPs and trehalose conjugation could improve the quality of conjugates LPs, which could expand their use in manufacturing as the acceptance of plant-based diets increases. PRACTICAL APPLICATION: Currently, lentil proteins (LPs) are used in plant-based protein powders and supplements. Though less popular than soy or pea proteins, LPs are valued for their high protein content and good amino acid profile. LPs are utilized in meat alternatives and high-protein snack products. The application of these products is mainly due to their nutritional benefits rather than functional properties due to their poor water solubility. Increasing the water solubility of LPs could significantly expand their application in various food industries, making LPs a more competitive and functional plant-based protein source. Trehalose-conjugated LPs with better water solubility allow LPs to be used in other food products, such as plant-based protein beverages. Better solubility would enhance the clarity and smoothness of these products, making them more appealing to consumers.