| Autor: |
Sorokina L; Nofima AS-Norwegian Institute of Food, Fisheries and Aquaculture Research, PB 210, N-1431 Ås, Norway. sileshi.wubshet@nofima.no.; Department of Chemistry, University of Oslo, Oslo, Norway., Solberg NT; Nofima AS-Norwegian Institute of Food, Fisheries and Aquaculture Research, PB 210, N-1431 Ås, Norway. sileshi.wubshet@nofima.no., Koga S; Nofima AS-Norwegian Institute of Food, Fisheries and Aquaculture Research, PB 210, N-1431 Ås, Norway. sileshi.wubshet@nofima.no., Rønning SB; Nofima AS-Norwegian Institute of Food, Fisheries and Aquaculture Research, PB 210, N-1431 Ås, Norway. sileshi.wubshet@nofima.no., Afseth NK; Nofima AS-Norwegian Institute of Food, Fisheries and Aquaculture Research, PB 210, N-1431 Ås, Norway. sileshi.wubshet@nofima.no., Wilson SR; Department of Chemistry, University of Oslo, Oslo, Norway., Rieder A; Nofima AS-Norwegian Institute of Food, Fisheries and Aquaculture Research, PB 210, N-1431 Ås, Norway. sileshi.wubshet@nofima.no., Wubshet SG; Nofima AS-Norwegian Institute of Food, Fisheries and Aquaculture Research, PB 210, N-1431 Ås, Norway. sileshi.wubshet@nofima.no. |
| Abstrakt: |
Bioactive peptides derived from food are promising health-promoting ingredients that can be used in functional foods and nutraceutical formulations. In addition to the potency towards the selected therapeutic target, the bioavailability of bioactive peptides is a major factor regarding clinical efficacy. We have previously shown that a low molecular weight peptide fraction (LMWPF) from poultry by-product hydrolysates possesses angiotensin-1-converting enzyme (ACE-1) and dipeptidyl-peptidase 4 (DPP4) inhibitory activities. The present study aimed to investigate the bioavailability of the bioactive peptides in the LMWPF. Prior to the investigation of bioavailability, a dipeptide YA was identified from this fraction as a dual inhibitor of ACE-1 and DPP4. Gastrointestinal (GI) stability and intestinal absorption of the bioactive peptides ( i.e. , YA as well as two previously reported bioactive dipeptides (VL and IY)) in the LMWPF were evaluated using the INFOGEST static in vitro digestion model and intestinal Caco-2 cell monolayer, respectively. Analysis of peptides after in vitro digestion confirmed that the dipeptides were resistant to the simulated GI conditions. After 4 hours of incubation, the concentration of the peptide from the apical side of the Caco-2 cell monolayer showed a significant decrease. However, the corresponding absorbed peptides were not detected on the basolateral side, suggesting that the peptides were not transported across the intestinal monolayer but rather taken up or metabolized by the Caco2 cells. Furthermore, when analyzing the gene expression of the Caco-2 cells upon peptide stimulation, a down-regulation of peptide transporters, the transcription factor CDX2 , and the tight junction protein-1 ( TJP1 ) was observed, suggesting the specific effects of the peptides on the Caco-2 cells. The study demonstrated that bioactive dipeptides found in the LMWPF were stable through in vitro GI digestion; however, the overall bioavailability may be hindered by inadequate uptake across the intestinal barrier. |
