Physicochemical and emulsifying properties of mussel water-soluble proteins as affected by lecithin concentration

July 30, 2020

Title

Physicochemical and emulsifying properties of mussel water-soluble proteins as affected by lecithin concentration

Author

Henan Zou, Ning Zhao, Sihui Li, Shuang Sun, Xinran Dong, Cuiping Yu

Year

2020

Journal

International Journal of Biological Macromolecules

Abstract

The effects of lecithin addition at different concentrations (0–2.0%) on the physicochemical and emulsifying properties of mussel water-soluble proteins (MWP) were investigated. In solution system, low lecithin concentration (0.5%–1.0%) induced the aggregation and increased turbidity of composite particles. Lecithin addition caused changes in secondary structure and induced partial unfolding of MWP. Hydrophobic interactions between MWP and lecithin may contribute to the exposure of chromophores and hydrophobic groups of MWP. The interfacial tension decreased with lecithin addition. However, at a high lecithin concentration (1.5%–2.0%), the degree of aggregation and state of unfolding alleviated due to competitive adsorption. In emulsion system, with the low concentration of lecithin addition (0.5%–1.0%), droplet size and surface charge of emulsion decreased. The emulsion activity index, emulsion stability index, percentage of adsorbed protein increased. Both creaming stability and viscoelastic properties improved. At an intermediate lecithin concentration (1.0%), the emulsion showed the highest physical stability, while further addition of lecithin caused a slight deterioration in emulsifying properties. Overall, these results indicated the possibility that the lecithin-MWP mixed emulsifiers can be used to obtain emulsions with desirable properties.

Instrument

J-810

Keywords

Circular dichroism, Protein folding, Secondary structure, Chemical stability, Biochemistry