Anti-Inflammatory Protein Hydrolysate Screened from Crayfish Shells Attenuates Colitis by Oxidative Stress Suppression, Inflammation Reduction and Barrier Reconstruction.
- 1School of Life and Health Sciences, Hubei University of Technology, No. 28 Nanli Road, Wuhan 430068, China.
- 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 -