Ultrasound-assisted pH-shifting to construct a stable aqueous solution of paprika oleoresin using egg yolk low-density lipoprotein as a natural liposome-like nano-emulsifier.

In this study, a stable aqueous solution of paprika oleoresin (PO, the natural colorant extracted from the fruit peel of Capsicum annuum L) was constructed. The solubility of PO in an alkline aqueous solution (pH 10.95-11.10) increased rapidly. However, the aqueous solution of PO (pH 12.00) was unstable, obvious stratification was observed, and the color retention rate was only 52.99% after 28 days of storage. Chicken egg yolk low-density lipoprotein (LDL) was added combined with ultrasonic treatment to improve the stability of LDL-PO solution. The method could decrease the turbidity by 17.5 %, reduce the average particle size of the LDL-PO solution (13.9%), and enhance the interaction and combination of LDL and PO. The prepared PO aqueous solution was used in yogurt, egg white gel, fish balls and soymilk, and it could significantly improve the color of products and provided potential health benefits.

Ultrasound-assisted pH-shifting remodels egg-yolk low-density lipoprotein to enable construction of a stable aqueous solution of vitamin D3.

Egg-yolk low-density lipoprotein (LDL) has a natural liposome structure. Using ultrasound-assisted pH-shifting (pH 12), a naturally safe and stable aqueous solution of vitamin D3 (VD3) was constructed employing LDL as the carrier. Images from electron microscopy showed that pH-shifting remodeled LDL molecules, resulting in a dramatic reduction in particle size (∼50%) and an increase in specific surface area, which reduced the turbidity (27.7%) and provided new interfaces for VD3 loading. Fluorescence analyses showed that the binding of VD3 to LDL under pH-shifting was strong, involved quenching, and the binding constant was 6.19 × 104 M-1. Thermogravimetric analysis and Fourier transform-infrared spectroscopy showed that pH-shifting hydrolyzed the esters in LDL to fatty acid salts, and the maximum weight loss of LDL occurred from 381.9 °C to 457.0 °C. Ultrasonic treatment enhanced the binding of LDL and VD3 (binding constant increased to 2.56 × 107 M-1), reduced the particle size, and increased the ζ-potential of the complex between LDL and VD3, thereby resulting in the improvement of solution stability and storage stability of VD3. Ultrasound-assisted pH-shifting could remodel LDL to construct a stable aqueous solution of VD3, which showed the potential of LDL as a carrier for lipid-soluble components.

Quantitative proteomic analyses during formation of chicken egg yolk.

A quantitative comparison of the proteomes during different periods of the formation of egg yolk, from yellow follicles (YF), small hierarchical follicles (9-12 mm, SF), and the largest hierarchical follicle (LF), was performed. The abundance of major egg yolk proteins (apolipoprotein B and vitellogenins) changed significantly during the yolk formation, and several protein hydrolases and isomerases, which may be related to the processing of egg yolk proteins, also varied significantly. The binding proteins for three vitamins (retinol, riboflavin, and vitamin D) and cholesterol were all most abundant in the LF period, suggesting that these nutrients were transported mainly at the final period of the egg yolk formation. Immunoglobulins decreased and complement proteins increased as formation progressed, indicating the dynamic nature of the egg yolk immune system. These results are helpful for understanding the nutrient composition, the formation of assembly structure, the preservation and processing properties of egg yolk.