Trehalose-conjugated lentil-casein protein complexes prepared by structural interaction: Effects on water solubility and protein digestibility

Food Chem. 2024 Jul 30:447:138882. doi: 10.1016/j.foodchem.2024.138882. Epub 2024 Feb 27.

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.

Keywords: Casein proteins; Digestibility; Lentil proteins; Protein structure; Trehalose; Water solubility.

MeSH terms

  • Caseins* / metabolism
  • Lens Plant* / chemistry
  • Solubility
  • Trehalose
  • Water / chemistry

Substances

  • Caseins
  • Trehalose
  • Water