The poor thermal and acid stabilities of anthocyanins greatly limit their industrial applications as functional food ingredients. This work investigated the ability of the Maillard reaction products (MRPs) of whey protein isolates and glucose to enhance the thermal stability of anthocyanins over the pH range of 2.0-7.0. Anthocyanin dispersions were subjected to up to 120 min of thermal treatment at 80 °C. The improvement in the color stability and antioxidant capacity of the anthocyanin dispersions indicated that MRP remarkably inhibited anthocyanin degradation. Fluorescence spectroscopy results suggested that anthocyanins and MRPs form complexes through hydrophobic interactions. These complexes effectively attenuated anthocyanin degradation under heat treatment at pH 6.0. The particle sizes of MRPs alone or in complex with anthocyanins remained unchanged after heating. The novel protein delivery system proposed in this study expands the applications of anthocyanins as acid- and heat-stable functional food ingredients.
In this study, whey protein isolates
(WPI), lactose (Lac) Maillard-reacted
products, and epigallocatechin gallate (EGCG) complex were used to
enhance the thermal stability of the Pickering emulsion delivery of
curcumin. Atomic force microscopy combined with Fourier transform
infrared spectroscopy were employed to study the morphological characteristics
and structural changes of WPI-Lac/EGCG nanoparticles. Results proved
that WPI-Lac and EGCG were combined by hydrogen bonding and hydrophobic
interaction. The mechanism underlying WPI-Lac/EGCG-stabilized Pickering
emulsion was further characterized by confocal laser scanning microscopy.
The optimal binding ratio of WPI-Lac to EGCG was 1:1 (w/w) at pH 3.0.
The particle size and zeta potential of the WPI-Lac/EGCG nanoparticles
were about 110 nm and 27 mV, respectively. Analysis of microstructure
and droplet size distribution revealed that the glycated WPI-Lac/EGCG-stabilized
emulsions exhibited more uniform droplet distribution, stronger thermal
stability, and higher curcumin percentage retention than WPI. These
results indicate that the WPI-Lac/EGCG nanoparticles are potential
stabilizers for Pickering emulsion requirements. This study provides
a basis for the construction of Pickering emulsion systems while carrying
pro-/hydrophobic bioactive components.
Egg white proteins are an excellent source of nutrition, with high biological and technological values. However, their limited functional properties prevent their widespread industrial applications. In this study, the ovalbumin functionality was improved via glycation by Maillard reaction with d-lactose. The free amino groups and sodium dodecyl sulfate-polyacrylamide gel electrophoresis profile were determined, confirming that glycation occurred between ovalbumin and lactose. The emulsification of the conjugate was 2.69-fold higher than that of ovalbumin at pH 7.0 after glycation. The thermal stability also improved remarkably. The glycated protein products were used to form an oil-water nanoemulsion for polymethoxyflavone-rich aged orange peel oil. The resulting nanoemulsion showed good pH, thermal, and storage stabilities.
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