To address the challenges of natural enzyme instability and mass transfer limitations in traditional immobilization techniques, this study proposes a sacrificial template strategy to develop cage-like nanogels (GNI-TG) that integrate efficient substrate transport with enzyme conformation protection, significantly enhancing enzyme stability and catalytic efficiency. The study employed methacrylated/quaternized dual-modified dextrin (MQD) to construct the continuous matrix of the nanogel, while designing Ca 2+ -ethylenediaminetetraacetic acid (EDTA) dynamic-responsive oxidized sodium alginate (OSA) as the sacrificial template. Structural analysis confirmed that the OSA and MQD formed a stable TG-protected structure through synergistic cross-linking mechanisms involving covalent Schiff base bonding and non-covalent interactions. GNI-TG retained 70 % of initial enzyme activity while demonstrating exceptional thermal stability (>50 % activity after 70 °C treatment) and broad pH adaptability (>70 % activity within pH 4–9). Leveraging polysaccharide-protein synergistic effects, GNI-TG significantly enhanced the comprehensive performance of whey protein/gelatin hydrogels. Compared to physically crosslinked and free TG crosslinked systems, CNI-TG crosslinked hydrogels exhibited superior gel strength (536.4 g), compressive strength (28.12 kPa), water-holding capacity (>99 %), thermal stability (T m = 138.4 °C), elastic behavior (G' > 1500 Pa), and network recovery (96.3 % recovery rate). This study establishes an enzyme immobilization paradigm through covalent anchoring, electrostatic assembly, and sacrificial templating strategies, demonstrating broad applicability in food processing, biocatalysis, and biomedical fields.
Biflavonoids are a kind of polyphenol compounds with numerous biological functions. However, the potential inhibitory activities of biflavonoids on α-glucosidase are yet unknown. Here, the inhibitory effects of two biflavonoids (amentoflavone and hinokiflavone) on α-glucosidase and their interaction mechanisms were explored using multispectral approaches and molecular docking. The results showed that the inhibitory activities of biflavonoids were much better compared with monoflavonoid (apigenin) and acarbose, and the order of inhibition ability was hinokiflavone > amentoflavone > apigenin > acarbose. These flavonoids were noncompetitive inhibitors of α-glucosidase and showed synergistic inhibition effects with acarbose. Additionally, they could statically quench the intrinsic fluorescence of α-glucosidase, and form the non-covalent complexes with enzyme primarily through hydrogen bonds and van der Waals forces. The binding of flavonoids changed the conformational structure of α-glucosidase, therefore impairing the enzyme activity. The findings suggested that biflavonoids could be considered as potential hypoglycemic functional foods in diabetes therapy.
The interaction of nanocarriers with gastrointestinal enzymes upon oral administration significantly impacts their performance as delivery systems. This work investigated the interaction between epigallocatechin gallate (EGCG) loaded into banana resistant starch nanoparticles (RSNPs) and digestive enzymes and its implications for EGCG release. The formation of a protein corona on EGCG-RSNPs in simulated gastrointestinal fluids was confirmed. The formation of this protein corona led to structural alterations in the pepsin and trypsin. Changes in enzyme conformation upon interaction with EGCG-RSNPs were elucidated using UV–Vis absorption and emission fluorescence spectroscopy. The activity of the enzymes remained largely unaffected despite these conformational changes. Additionally, the presence of the protein corona led to a slower, reduced release rate of EGCG. The results of this work will contribute to the growing knowledge of nanocarrier design for the delivery of bioactive compounds, paving the way for the development of innovative therapeutic strategies and functional foods with more excellent health benefits.
危险品化学品经营许可证（带存储）