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Comparison of the inhibitory effects of procyanidins with different structures and their digestion products against acrylamide-induced cytotoxicity in IPEC-J2 cells
- Source :
- Journal of Functional Foods, Vol 72, Iss, Pp 104073-(2020)
- Publication Year :
- 2020
- Publisher :
- Elsevier, 2020.
-
Abstract
- This study evaluated the stabilities of catechin (C), epicatechin (EC), procyanidin B3, procyanidin A1 and epicatechin-(4β → 6)-epicatechin-(2β → O → 7,4β → 8)-catechin (PCA-trimer) during in vitro digestion, as well as characterized their digestion products (DPs), and evaluated their protective effects against ACR-induced cytotoxicity on IPEC-J2 cells. The results showed that procyanidin A1 (70.38%) and procyanidin B3 (15.25%) had the highest and lowest stability in the gastric phase, respectively. During the intestinal phase, the contents of C, EC and procyanidin B3 increased from 57.37%, 49.92% and 15.25% to 88.15%, 71.81% and 46.72%, while those of procyanidin A1 and PCA-trimer showed continuous decreases to 27.13% and 28.89%, respectively. Isomerism, hydrolysis and condensation reactions were found to play major roles in in vitro digestion. Besides, procyanidin A1 and its DPs exhibited the best protective effect against ACR-induced cytotoxicity compared with other compounds and their DPs, as indicated by MTT assay and measurement of glutathione (GSH).
- Subjects :
- 0301 basic medicine
Medicine (miscellaneous)
03 medical and health sciences
chemistry.chemical_compound
0404 agricultural biotechnology
MTT assay
TX341-641
Food science
Procyanidin B3
Cytotoxicity
Procyanidins
Acrylamide
030109 nutrition & dietetics
Nutrition and Dietetics
Chemistry
Nutrition. Foods and food supply
In vitro digestion
Catechin
04 agricultural and veterinary sciences
Glutathione
040401 food science
IPEC-J2 cells
Digestion
Procyanidin A1
(Epi)catechin
Food Science
Subjects
Details
- Language :
- English
- ISSN :
- 17564646
- Volume :
- 72
- Database :
- OpenAIRE
- Journal :
- Journal of Functional Foods
- Accession number :
- edsair.doi.dedup.....d0dca18fd14f0a3e6479999367495407