Lentil protein and trehalose conjugates: Structural interactions and mechanisms for improving multi-level structure and functional characteristics
| dc.contributor.author | Alrosan, Mohammad | |
| dc.contributor.author | Maghaydah, Sofyan | |
| dc.contributor.author | Al-Qaisi, Ali | |
| dc.contributor.author | ETAL.. | |
| dc.date.accessioned | 2025-09-08T09:07:29Z | |
| dc.date.available | 2025-09-08T09:07:29Z | |
| dc.date.issued | 2024 | |
| dc.description | Protein digestibility is critical in determining protein quality because it breaks down the protein into amino acids for absorption and utilization (Orlien et al., 2023). Plant-based proteins have lower digestibility: lentil proteins (LPs, 76.42%, Alrosan et al., 2021), quinoa proteins (78.54%, Alrosan et al., 2022a), and chickpea proteins (63.62%, Liu et al., 2023), compared to animal-based proteins: whey (88.48%, Alrosan et al., 2022a) and casein (83.7%, Almeida et al., 2015). Several factors affect plant-based protein digestibility, including the amino acid profile, fiber content, anti-nutritional agents, extraction process, and physical form (Jarpa-Parra et al., 2017). LPs are predominantly globulins and contain certain anti-nutritional factors, such as phytic acid and enzyme inhibitors (Jarpa-Parra et al., 2014, 2017). | |
| dc.description.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. keywords: functional characteristics, protein, Structural interactions , mechanisms for improving multi-level structure, trehalose conjugates | |
| dc.identifier.citation | Alrosan, M., Maghaydah, S., Al‐Qaisi, A., Almajwal, A. M., Alu'datt, M. H., Qudsi, F. R. A., ... & Mahmood, A. A. R. (2024). Lentil protein and trehalose conjugates: Structural interactions and mechanisms for improving multi‐level structure and functional characteristics. Journal of Food Science, 89(12), 8887-8899. | |
| dc.identifier.doi | https://doi.org/10.1111/1750-3841.17465 | |
| dc.identifier.uri | https://repository.adu.ac.ae/handle/1/7389 | |
| dc.language.iso | en | |
| dc.publisher | Wiley | |
| dc.title | Lentil protein and trehalose conjugates: Structural interactions and mechanisms for improving multi-level structure and functional characteristics | |
| dc.type | Article |