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
This study aimed to assess the technique of natural fermentation by applying water kefir to the casein protein. The diverse microorganisms and their enzymes found naturally in the water kefir can influence casein's characteristics. The fermented casein's protein quality (digestibility and secondary protein structure) and composition (total soluble solids and nutritive and non-nutritive substances) were investigated. Our findings revealed that the fermented casein's protein digestibility and total phenolic content increased from 82.46 to 88.60 % and 7.6 to 8.0 mg gallic acid equivalent/100 g, respectively. In addition, their surface charge and hydrophobicity changed from -30.06 to -34.93 mV and 286.9 to 213.7, respectively. Furthermore, the fermented casein's secondary protein components, α-helix (decreased from 13.66 to 8.21 %) and random coil (increased from 16.88 to 19.61 %), were also altered during the fermentation. Based on these findings, the water kefir fermentation approach could be an effective, practical, non-thermal approach for improving casein's protein quality and composition.
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