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Evaluation of digestibility, solubility, and surface properties of trehalose-conjugated quinoa proteins prepared via pH shifting technique

2024; Elsevier BV; Volume: 22; Linguagem: Inglês

10.1016/j.fochx.2024.101397

2590-1575

Mohammad Alrosan, Ali Almajwal, Ali Al‐Qaisi, Sana Gammoh, Muhammad H. Alu’datt, Farah R. Al Qudsi, Thuan‐Chew Tan, Ammar A. Razzak Mahmood, Sofyan Maghaydah, Motasem Al-Massad,

Microbial Metabolites in Food Biotechnology

Soluble trehalose-conjugated quinoa proteins (T-QPs) were effectively prepared using the pH-shifting mechanism. The structural properties of the T-QPs were evaluated using a comparative evaluation, which included analyzing the amide I, surface charge and hydrophobicity, protein conformation, thermal stability, and protein structures. The results suggested that the development of the T-QPs was influenced mainly by no-covalent bonds. These interactions significantly influenced (P < 0.05) the quinoa proteins' conformation and higher-protein structure. T-QP had significant (P < 0.05) surface properties. Furthermore, the T-QPs exhibited improved solubility (79.7 to 88.4%) and digestibility (79.8 to 85.1%). Therefore, quinoa protein proved an excellent plant-based protein for conjugation with disaccharides. These findings provide significant insight into the potential development of modified proteins with enhanced solubility and digestibility by creating trehalose-conjugated plant-based proteins.