The Effects of Ethanol and Rutin on the Structure and Gel Properties of Whey Protein Isolate and Related Mechanisms

Abstract

The effects of different levels of rutin (0, 0.05%, 0.1%, 0.2% and 0.3% w/v) and ethanol on the structure and gel properties of whey protein isolate (WPI) were examined. The results showed that the addition of ethanol promoted the gel formation of WPI. The addition of rutin increased the gel strength of WPI and maintained the water-holding capacity of the gel. Ethanol caused an increase in thiol content and surface hydrophobicity, but rutin decreased the thiol content and surface hydrophobicity of WPI. The particle size, viscosity and viscoelasticity of WPI increased at rutin levels of 0.2% and 0.3%, indicating that rutin caused cross-linking and aggregation of WPI, but rutin had no significant effect on the zeta-potential, indicating that electrostatic interactions were not the main force causing the changes in protein conformation and gel properties. Ethanol and rutin improved the gel properties of WPI possibly by inducing cross-linking of WPIs via hydrophobic and covalent interactions.

Interactions between intestinal microbial fermentation products of Pleurotus eryngii polysaccharide with gut mucus

“…When the absolute value of the zeta potential is low, the surface charge of the molecule in the solution is less, the electrostatic repulsion between the molecule is reduced, and the particles in the solution tend to accumulate, making the molecule surface hydrophobic. 30 The electrostatic interaction force between FPEP and IM was shown by measuring zeta potential.…”

“…Under electrostatic and hydrophobic interactions, unfolded polypeptide chains and exposed hydrophobic groups can easily form aggregates under both forces and charged amino acids are rearranged on the surface of the aggregates, leading to an increase in the absolute zeta potential. 30 The complex action of molecules of different sizes in solution leads to a decrease in zeta potential at that time point and an insignificant effect of IM on the potential, which is also a drawback of this study.…”

“…Food & Function molecule is reduced, and the particles in the solution tend to accumulate, making the molecule surface hydrophobic. 30 The electrostatic interaction force between FPEP and IM was shown by measuring zeta potential. It can be observed from Fig.…”

The Effect of Ethanol on Lipid Nanoparticle Stabilization from a Molecular Dynamics Simulation Perspective

“…The interaction between ethanol and lipids involves the dissolution of lipids in ethanol due to its hydrophobic nature, which reduces lipid packaging and potential changes in lipid structure. Ethanol is less polar and has a lower dielectric constant than water, which makes it easy to break non-covalent interactions like hydrogen bonds or hydrophobic interactions [ 22 ]. Ethanol can act as a cosolvent, reducing the strength of the interactions between the lipids and causing the LNP structure to become less stable.…”