Molecular forces driving protein complexation of lentil and whey proteins: Structure-function relationships of trehalose-conjugated protein complexes on protein digestibility and solubility

• Published in: Current research in structural biology 2024-01, Vol.7, p.100135-100135, Article 100135
• Main Authors: Alrosan, Mohammad, Madi Almajwal, Ali, Al-Qaisi, Ali, Gammoh, Sana, H. Alu'datt, Muhammad, R. Al Qudsi, Farah, Tan, Thuan-Chew, A. Razzak Mahmood, Ammar, Maghaydah, Sofyan
• Format: Article
• Language: English
• Subjects: Digestibility; Disaccharide; Lentil proteins; Protein structure; Whey proteins
• ISSN: 2665-928X; 2665-928X
• DOI: 10.1016/j.crstbi.2024.100135

Plant-based proteins are often associated with a range of health benefits. Most research primarily investigates pea and soy proteins, while lentil proteins received minimal attention. This study evaluates the effect of protein complexation (using the pH-shifting technique) coupled with trehalose conjugation on lentil and whey proteins. The protein structures after the modification were analysed using spectroscopic methods: Fourier-transform infrared, ultraviolet spectra, and fluorescence spectra. The amide group I, conformation protein, and tertiary structure of the trehalose-conjugated lentil-whey protein complexes (T-LWPs) showed significant changes (P < 0.05). Moreover, the surface properties (surface hydrophobicity and charges) of T-LWPs were significantly modified (P < 0.05), from 457 to 324 a.u and from 36 to −40 mV, respectively. Due to these modifications on the protein structures, the protein digestibility (80–86%) and water solubility (90–94.5%) of T-LWPs increased significantly (P