Hydrophobic bioactives (e.g., curcumin, carotenoids, polyphenols) offer substantial health benefits but are fundamentally limited by poor water solubility, environmental instability, and low gastrointestinal bioavailability. While colloidal delivery systems help overcome these barriers, current research typically isolates and optimizes individual platforms, neglecting the broader conflict between structural stability and digestive bioaccessibility. This review systematically compares three hierarchical spatial confinement strategies-two-dimensional Pickering emulsions (PEs), three-dimensional macroscopic emulsion gels (EGs), and three-dimensional nanogels (NGs)-to clarify their structure-function relationships. We identify a fundamental tradeoff: structural features that maximize environmental stability often create severe steric hindrance, restricting enzyme permeability and lipid micellization. Consequently, release mechanisms vary fundamentally across platforms: PEs rely on interfacial desorption (first-order kinetics), EGs use continuous matrix diffusion (Ritger-Peppas model) for sustained release, and NGs leverage stimuli-responsive dynamic dissociation. Additionally, we map compound-specific compatibility requirements, showing that curcumin needs interfacial physical masking against alkaline hydrolysis, carotenoids require nanoscale amorphous confinement to prevent photo-oxidation, and polyphenols depend on dynamic redox protection. To address current bottlenecks, we advocate shifting from "passive stabilization" to "digestion-responsive engineering." By examining critical hurdles like the lack of in vitro-in vivo correlation (IVIVC), scalability, and long-term nanotoxicity, this review provides a practical framework for designing next-generation delivery systems.
Congxi Xu, Weiwei Cheng, Xinshuai Zhang et al.· Critical reviews in food sci...· 0 citations
Pea protein offers valuable nutritional and environmental advantages, yet its application in food emulsions is hindered by poor solubility and emulsifying capacity—a consequence of its inherently aggregated and rigid structure. To address this limitation, the present study developed a dual modification strategy combining controlled enzymatic hydrolysis (DH 3%) with heat assisted pH shifting. PPI was first hydrolyzed with either trypsin or pepsin, then subjected to pH 3 or pH 9 at 70°C. Trypsin hydrolysis proved markedly more effective than pepsin treatment, generating fragments with enhanced surface hydrophobicity, reduced aggregate size (~280 nm), and improved solubility, dispersibility, and emulsifying performance—benefits attributable to the stringent cleavage specificity of trypsin for lysine and arginine residues. Subsequent alkaline pH shifting (pH 9) with heating further exploited electrostatic repulsion to dissociate the aggregates to ~160 nm, yielding additional functional gains. In contrast, acidic pH shifting (pH 3) under the same heating conditions promoted extensive protein reaggregation and conferred no functional benefit. The optimally modified PPI—obtained by combining trypsin hydrolysis with alkaline pH shifting—enabled formulation of submicron sized oil in water emulsions (D_4,3=0.607±0.001 μm). These emulsions withstood 30 days of storage (D_4,3=0.837±0.003 μm) and heating at 95°C for 60 min (D_4,3=1.18±0.05 μm) with only modest droplet size increases, demonstrating notable stability. This work establishes that the synergy between enzymatic digestion and alkaline pH shifting effectively dissociates protein aggregates while avoiding the generation of excessively small peptides that would compromise emulsion stability. The dual strategy thus transforms pea protein into an efficient molecular emulsifier, offering a promising route for developing advanced plant based ingredients.
Kai Zhang, Yue Ding, Xinshuai Zhang et al.· Chiang Mai Journal of Scienc...· 0 citations
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