Transglutaminase-Crosslinked Collagen Gel Delays Gastrointestinal Transit and Prolongs Serum Appearance of Antioxidant Collagen Di- and Tripeptides in Mice
- 1College of Food Science, Southwest University, Chongqing 400715, China
- 2Chongqing Academy of Agricultural Sciences, Chongqing 401329, China
Abstract
Background: Transglutaminase-crosslinked collagen gel (CHG) is a collagen product cross-linked with transglutaminase (TGase) that exhibits good thermal stability and has potential applications in functional food formulations. However, it remains unclear whether the gelation of CHG alters the metabolic fate of collagen-derived bioactive peptides in the gastrointestinal tract and their distribution within the body. Methods: This study investigated the retention of CHG in the gastrointestinal tract of male C57BL/6J mice, as well as its serum peptide levels and antioxidant activity. Results: Compared with unhydrolyzed (CNS) and hydrolyzed collagen (CHS) sols, CHG significantly prolonged gastric retention and slowed intestinal transit, while gastric contents exhibited larger particle sizes and a more sustained release of protein. The CHG also increased the expression of genes associated with Cajal interstitial (ICC) cells in the gastric antrum (HCN1, Trpm7, CX43, and c-kit) and prolonged the secretion of leptin, cholecystokinin, serotonin, and vasoactive intestinal peptide. Serum peptide analysis showed that the concentrations of most collagen dipeptides and tripeptides, peaked between 0.5 and 1.5 h and then gradually declined; notably, the concentration of Pro-Hyp in the CHG group remained higher than that in the control group at 3 h, indicating prolonged serum appearance. Serum peptides from CHG group (particularly Pro-Hyp) exhibited total antioxidant capacity and hydroxyl radical scavenging activity, and the mixed-peptide solution significantly reduced the accumulation of reactive oxygen species in H2O2-induced skin fibroblasts (p < 0.001). Conclusions: These findings suggest that the cross-linked structure of CHG alters gastrointestinal metabolic processes and is associated with the persistent presence of collagen-derived dipeptides and tripeptides in serum.
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BibTeX
@article{lu2026transglutaminasecrosslinked,
title = {{Transglutaminase-Crosslinked Collagen Gel Delays Gastrointestinal Transit and Prolongs Serum Appearance of Antioxidant Collagen Di- and Tripeptides in Mice}},
author = {Yapeng Lu and Ying He and Xin Feng and Mi Yan and Yexing Liang and Liang Ma and Yuhao Zhang},
journal = {Nutrients},
year = {2026},
month = oct,
doi = {10.3390/nu18213602},
url = {https://www.mdpi.com/2072-6643/18/21/3602},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Transglutaminase-Crosslinked Collagen Gel Delays Gastrointestinal Transit and Prolongs Serum Appearance of Antioxidant Collagen Di- and Tripeptides in Mice
AU - Yapeng Lu
AU - Ying He
AU - Xin Feng
AU - Mi Yan
AU - Yexing Liang
AU - Liang Ma
AU - Yuhao Zhang
PY - 2026
DA - 2026/10/30
JO - Nutrients
DO - 10.3390/nu18213602
UR - https://www.mdpi.com/2072-6643/18/21/3602
AB - Background: Transglutaminase-crosslinked collagen gel (CHG) is a collagen product cross-linked with transglutaminase (TGase) that exhibits good thermal stability and has potential applications in functional food formulations. However, it remains unclear whether the gelation of CHG alters the metabolic fate of collagen-derived bioactive peptides in the gastrointestinal tract and their distribution within the body. Methods: This study investigated the retention of CHG in the gastrointestinal tract of male C57BL/6J mice, as well as its serum peptide levels and antioxidant activity. Results: Compared with unhydrolyzed (CNS) and hydrolyzed collagen (CHS) sols, CHG significantly prolonged gastric retention and slowed intestinal transit, while gastric contents exhibited larger particle sizes and a more sustained release of protein. The CHG also increased the expression of genes associated with Cajal interstitial (ICC) cells in the gastric antrum (HCN1, Trpm7, CX43, and c-kit) and prolonged the secretion of leptin, cholecystokinin, serotonin, and vasoactive intestinal peptide. Serum peptide analysis showed that the concentrations of most collagen dipeptides and tripeptides, peaked between 0.5 and 1.5 h and then gradually declined; notably, the concentration of Pro-Hyp in the CHG group remained higher than that in the control group at 3 h, indicating prolonged serum appearance. Serum peptides from CHG group (particularly Pro-Hyp) exhibited total antioxidant capacity and hydroxyl radical scavenging activity, and the mixed-peptide solution significantly reduced the accumulation of reactive oxygen species in H2O2-induced skin fibroblasts (p < 0.001). Conclusions: These findings suggest that the cross-linked structure of CHG alters gastrointestinal metabolic processes and is associated with the persistent presence of collagen-derived dipeptides and tripeptides in serum.
SN - 2072-6643
ER -