AI Article Synopsis
- The formation of the ovalbumin-gum arabic complex leads to enhanced crystal structure and increased protein denaturation temperature from 72 to 96 °C.
- Gum arabic reduces pH-induced disruptions in ovalbumin's structure, stabilizing its α-helix and β-turn regions more effectively than other domains.
- The optimal viscosity of the coacervate occurs at pH 3.7 due to stronger interactions, and variations in salt concentration and OVA:GA ratios also significantly affect the rheological properties of the complexes.
Article Abstract
After formation of the ovalbumin (OVA)-gum arabic (GA) complex coacervates, a more ordered crystal structure was obtained, and the protein denaturation temperature increased from 72 to 96 °C. GA can reduce the pH-induced conformational perturbations of ovalbumin. The presence of GA improved the stability of the α-helix and β-turn regions against pH, but showed less influence on the random coil and β-sheet domains. The complex coacervates showed the highest viscosity value at pH 3.7 compared with the other pH values tested (4.0, 3.4, 3.0, 2.7) due to the stronger interactions of OVA and GA. A large thixotropic loop was observed for the coacervate obtained at pH 3.7 compared with that obtained at pH 4.0. Moreover, the salt concentration and OVA:GA ratio influenced the rheological properties by affecting the structure and composition of the complexes. A stronger interaction between OVA and GA led to greater viscoelastic properties.
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| http://dx.doi.org/10.1016/j.foodchem.2018.03.141 | DOI Listing |
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