Trehalose-conjugated lentil-casein protein complexes prepared by structural interaction: Effects on water solubility
Mohammad Alrosan1, Ali Madi Almajwal2, Ali Al-Qaisi3
1Food Technology Division, School of Industrial Technology, Universiti Sains Malaysia, 11800 USM, Penang, Malaysia; Applied Science Research Center, Applied Science Private University, Al-Arab St. 21, Amman 11931, Jordan; College of Health Science, QU Health, Qatar University, Doha P.O. Box 2713, Qatar; Department of Nutrition and Food Science, Faculty of Agriculture, Jerash University, Jerash, Jordan.
Abstract:
The two limiting factors for lentil protein utilization are water solubility and digestibility. In this study, we utilized two non-thermal techniques: (1) protein complexation of lentil and casein proteins using the pH-shifting method and (2) protein conjugation with trehalose to produce trehalose-conjugated lentil-casein protein complexes (T-CPs) with enhanced water solubility and digestibility. The protein structure of the T-CPs was analyzed for secondary protein structure, conformation protein, and tertiary protein structure using Fourier-transform infrared, UV, and fluorescence spectroscopies, respectively. The surface hydrophobicity and surface charge of T-CPs solution at pH 7.0 changed significantly (P < 0.05). Using these two non-thermal techniques, the water solubility and digestibility of T-CPs increased significantly (P < 0.05) by 85 to 89 % and 80 to 85 %, respectively. The results of this study suggested that these non-thermal techniques could enhance the surface and protein structure properties, improving water solubility and digestibility.
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