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Yugui Wang

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Open access Aug 2026

Isolation, gastrointestinal stability, intestinal transport, and allergenicity of antioxidant peptides derived from crocodile (Crocodylus siamensis) blood proteins.

Antioxidant peptides derived from crocodile blood remain poorly characterized, regarding defined sequences, gastrointestinal stability, intestinal transport, and allergenicity. In this study, antioxidant peptides were generated from crocodile (Crocodylus siamensis) blood proteins via enzymatic hydrolysis. Two peptides (MLHVGPEIAPL and AAHYPKDFGL), prepared by pepsin, exhibited strong antioxidant activity, with 1, 1-diphenyl-2-picrylhydrazyl (DPPH) radical-scavenging activity of 10.39-14.09 μmol Trolox equivalents (TE)/mg and reducing power of 2.43-5.00 μmol TE/mg. Simulated gastrointestinal digestion revealed that AAHYPKDFGL was further hydrolyzed into shorter peptides (AAHYPK and DFGL) with retained activity. These peptides could pass the Caco-2 monolayer with apparent permeability coefficients of 2.80-11.98 × 10-7 cm/s, despite being degraded by aminopeptidase N to varying degrees. They reduced cellular oxidative stress (decreased superoxide/malondialdehyde levels) without affecting major antioxidant enzymes. No significant allergenicity was detected for these peptides. These findings highlighted crocodile blood proteins as an underexplored source of antioxidant peptides for functional food application.

Zhiying Wang, Yugui Wang, Hui Hong et al. · 0 citations
Jul 2026

Concentration-dependent gelation, water-holding, and emulsifying performance of soybean peptide-hawthorn pectin Maillard hydrogels.

This study examined the concentration-dependent gelation and structural evolution of heat-induced hydrogels prepared from soybean peptide-hawthorn pectin Maillard reaction products (SBP-HP MRP). With increasing concentration, the system shifted from molecular association to network formation. Rheological measurements showed weak gel formation at approximately 9.0 mg/mL, whereas vial inversion identified 9.5 mg/mL as the self-supporting gel concentration. From 9.0 to 12.0 mg/mL, apparent cross-linking density increased from 3.54 to 6.63 mol·m - 3, and mesh size decreased from 73.58 to 50.84 nm, indicating progressive network densification. Avrami analysis and DLS suggested faster aggregate growth and larger aggregates at higher concentrations. Functional evaluation identified 11.0 mg/mL as the optimal concentration, showing high water-holding capacity (94%), EAI (≈34 m2/g), OHC (18%), and balanced texture. Excessive concentration increased rigidity but weakened functional performance. These findings clarify structure-function relationships in SBP-HP MRP hydrogels and support formulation design for texture-modified foods and delivery systems.

Xiaoshen Feng, Huanmei Meng, Huiyao Zhang et al. · 0 citations