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Trehalose-conjugated lentil-casein protein complexes prepared by structural interaction: Effects on water solubility and protein digestibility
[Display omitted] •Prepare soluble protein composite based on casein and lentil proteins (CPs).•Trehalose-conjugated PCs based on pH shifting.•CP-trehalose conjugates have a high solubility and digestibility. The two limiting factors for lentil protein utilization are water solubility and digestibil...
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Published in: | Food chemistry 2024-07, Vol.447, p.138882-138882, Article 138882 |
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Main Authors: | , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | [Display omitted]
•Prepare soluble protein composite based on casein and lentil proteins (CPs).•Trehalose-conjugated PCs based on pH shifting.•CP-trehalose conjugates have a high solubility and digestibility.
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 |
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ISSN: | 0308-8146 1873-7072 |
DOI: | 10.1016/j.foodchem.2024.138882 |