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Evaluation of polyphenol bioavailability in rat small intestine
M Carbonaro1, G Grant, A Pusztai
1Istituto Nazionale di Ricerca per gli Alimenti e la Nutrizione, Roma, Italy. carbonaro@inran.it
European Journal of Nutrition
|August 24, 2001
Summary
Dietary polyphenols like tannic acid and catechin interact with the gut. Only catechin is absorbed, suggesting polyphenols may be limited by protein binding, not protein digestion inhibition.
Area of Science:
- Gastroenterology
- Nutritional Science
- Pharmacology
Background:
- Dietary polyphenols show potential in preventing cardiovascular diseases and cancer.
- Limited and contradictory data exist regarding polyphenol absorption in the gastrointestinal tract.
Purpose of the Study:
- To evaluate polyphenol bioavailability using rat small intestine segments.
- To assess the absorption of tannic acid (high molecular weight) and catechin (low molecular weight) polyphenols.
- To examine the impact of tannic acid binding to bovine serum albumin (BSA) on absorption and protein digestibility.
Main Methods:
- Rat small intestine segments were incubated with varying concentrations of polyphenols.
- Polyphenol absorption was quantified by measuring luminal disappearance and transfer into the buffer.
- In vivo protein digestibility was assessed using BSA and a BSA-tannic acid complex.
Main Results:
- Both polyphenols showed concentration-dependent disappearance from the rat small intestine.
- Tannic acid uptake was higher (50%) than catechin (30%), but only catechin showed significant transfer (10%) into the buffer.
- Polyphenols bound to endogenous intestinal proteins, potentially limiting absorption.
- Tannic acid complexed with BSA did not affect its interaction with the intestine or protein digestibility.
Conclusions:
- Tannic acid and catechin interact with the gut, but only catechin is absorbed.
- Endogenous protein binding may limit polyphenol absorption in the small intestine.
- Tannic acid's anti-nutritional effects may stem from gut wall interactions rather than inhibiting dietary protein digestion.