Solubilization of Hydrophobic Astaxanthin in Water by Physical Association with Phytoglycogen Nanoparticles.

Astaxanthin (AXT) is a xanthophyll carotenoid with reported health benefits. Realizing its potential as a bioactive is challenging because of its extremely poor solubility in water. We describe a method to improve the effective solubility of AXT in water through its physical association with phytoglycogen (PG), which is produced in sweet corn as compact, highly branched nanoparticles. We combine PG in water with AXT in acetone, evaporate the acetone, and lyophilize. The result is an AXT-PG complex that can be readily redispersed in water, resulting in stable aqueous dispersions. By characterizing the UV-vis absorbance due to different aggregation states of AXT in the AXT-PG complex, we determined the maximum loading of AXT onto PG to be ∼10% by mass. Our results demonstrate the promise of using PG as a solubilizing agent for hydrophobic compounds in water.

Binding Affinity of Concanavalin A to Native and Acid-Hydrolyzed Phytoglycogen Nanoparticles.

Phytoglycogen (PG) is a polysaccharide produced in the kernels of sweet corn as soft, highly branched, compact nanoparticles. Its tree-like or dendritic architecture, combined with a high-safety profile, makes PG nanoparticles attractive for use in biological applications, many of which rely on the association or binding of small biomolecules. We have developed a methodology to functionalize surface plasmon resonance (SPR) sensor surfaces with PG nanoparticles, and we demonstrate the utility of the PG-functionalized SPR sensor by measuring the binding affinity of the tetrameric concanavalin A (ConA) protein to both native PG nanoparticles and smaller, softer acid-hydrolyzed PG nanoparticles. We measure comparable values of the equilibrium association constant K for native and acid-hydrolyzed PG, with a slightly smaller value for the acid-hydrolyzed particles that we attribute to unfavorable lateral interactions between the tetrameric subunits of ConA due to the increase in surface curvature of the smaller acid-hydrolyzed PG particles. We also use infrared reflection-absorption spectroscopy (IRRAS) to show that ConA maintains a large fraction of its native conformation, and thus its bioactivity, upon binding to PG, representing an important step toward the realization of PG as a novel bioactive delivery vehicle.