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Peer-reviewedCC BYFoods (Basel, Switzerland)

Anti-Inflammatory Protein Hydrolysate Screened from Crayfish Shells Attenuates Colitis by Oxidative Stress Suppression, Inflammation Reduction and Barrier Reconstruction.

  1. 1School of Life and Health Sciences, Hubei University of Technology, No. 28 Nanli Road, Wuhan 430068, China.
  2. 2College of Food Science and Engineering, Yangzhou University, Yangzhou 210095, China.

Abstract

Inflammatory bowel disease (IBD) is associated with intestinal inflammation and oxidative stress. Protein-rich crayfish shell (CS) by-products may provide a sustainable source of bioactive hydrolysates. This study screened five protease-derived hydrolysates and evaluated the alkaline protease-derived hydrolysate (ACSP) in lipopolysaccharide-stimulated IEC-6 cells and mice with DSS-induced colitis. ACSP scavenged DPPH and ABTS•⁺ radicals, with IC₅₀ values of 0.888 ± 0.004 and 0.853 ± 0.003 mg/mL. It also enhanced superoxide dismutase and catalase activities, and inhibited NO release and albumin denaturation in vitro. In IEC-6 cells, ACSP increased viability, reduced iNOS, IL-1β, IL-6, and TNF-α expression, and increased IL-10 expression. In mice, ACSP attenuated weight loss, disease activity, colon shortening, histopathological injury, and goblet cell depletion. The high-dose group had disease activity index and histological scores of 3.60 ± 0.55 and 4.80 ± 0.40 compared with 9.40 ± 1.14 and 10.40 ± 0.80 in the model group. ACSP reduced pro-inflammatory cytokines, myeloperoxidase activity, and NO levels while restoring antioxidant enzyme activities and tight junction protein expression. Peptidomic analysis identified 516 peptide sequences, including peptides containing hydrophobic, acidic, and C-terminal basic residues. These findings support further investigation of ACSP for intestinal health applications and the value-added utilization of CS by-products.

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BibTeX
@article{dong2026antiinflammatory,
  title = {{Anti-Inflammatory Protein Hydrolysate Screened from Crayfish Shells Attenuates Colitis by Oxidative Stress Suppression, Inflammation Reduction and Barrier Reconstruction.}},
  author = {Lei Dong and Hao Wang and Yongmin Wu and Jinyang Peng and Shaohao Lai and Zexin Zhao and Yongqi Yin and Jun Cai},
  journal = {Foods (Basel, Switzerland)},
  year = {2026},
  month = sep,
  doi = {10.3390/foods15193389},
  url = {https://europepmc.org/article/MED/42883496},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Anti-Inflammatory Protein Hydrolysate Screened from Crayfish Shells Attenuates Colitis by Oxidative Stress Suppression, Inflammation Reduction and Barrier Reconstruction.
AU  - Lei Dong
AU  - Hao Wang
AU  - Yongmin Wu
AU  - Jinyang Peng
AU  - Shaohao Lai
AU  - Zexin Zhao
AU  - Yongqi Yin
AU  - Jun Cai
PY  - 2026
DA  - 2026/09/23
JO  - Foods (Basel, Switzerland)
DO  - 10.3390/foods15193389
UR  - https://europepmc.org/article/MED/42883496
AB  - Inflammatory bowel disease (IBD) is associated with intestinal inflammation and oxidative stress. Protein-rich crayfish shell (CS) by-products may provide a sustainable source of bioactive hydrolysates. This study screened five protease-derived hydrolysates and evaluated the alkaline protease-derived hydrolysate (ACSP) in lipopolysaccharide-stimulated IEC-6 cells and mice with DSS-induced colitis. ACSP scavenged DPPH and ABTS•⁺ radicals, with IC₅₀ values of 0.888 ± 0.004 and 0.853 ± 0.003 mg/mL. It also enhanced superoxide dismutase and catalase activities, and inhibited NO release and albumin denaturation in vitro. In IEC-6 cells, ACSP increased viability, reduced iNOS, IL-1β, IL-6, and TNF-α expression, and increased IL-10 expression. In mice, ACSP attenuated weight loss, disease activity, colon shortening, histopathological injury, and goblet cell depletion. The high-dose group had disease activity index and histological scores of 3.60 ± 0.55 and 4.80 ± 0.40 compared with 9.40 ± 1.14 and 10.40 ± 0.80 in the model group. ACSP reduced pro-inflammatory cytokines, myeloperoxidase activity, and NO levels while restoring antioxidant enzyme activities and tight junction protein expression. Peptidomic analysis identified 516 peptide sequences, including peptides containing hydrophobic, acidic, and C-terminal basic residues. These findings support further investigation of ACSP for intestinal health applications and the value-added utilization of CS by-products.
SN  - 2304-8158
ER  -