Amélie Deglaire

Ileal digestibility of dietary protein in the growing pig and adult human

The suitability of the pig as an animal model for predicting protein digestibility in man was evaluated. Healthy adult human subjects (mean body weight 67 kg; n 11) and growing pigs (mean body weight 40 kg; n 15) were fed semi-synthetic mixed meals containing, as a sole source of N, casein (C), hydrolysed casein (HC) or rapeseed isolate (R). There was no prior adaptation to the test meal. Ileal digesta were sampled through a naso-ileal tube (human subjects) or a post-valve T-caecum cannula (pigs) after ingestion of a bolus meal. The protein sources were 15N-labelled. Amino acid (AA) digestibilities were not determined for R. Ileal apparent N digestibility was markedly lower (14-16 %; P < 0.001) in human subjects than in pigs (C, HC, R). Similarly, most apparent ileal AA digestibilities were lower (8 % on average; P < 0.05) in human subjects (C, HC). Ileal true N digestibility was slightly lower (3-5 %; P < 0.001) in human subjects than in pigs (C, HC, R) and most true ileal AA digestibilities were similar (P>0.05) between the species (C, HC). Exceptions were for phenylalanine, tyrosine, lysine, histidine and aspartic acid for which digestibilities were lower (3 % on average; P < 0.001) in human subjects. A similar ranking of the diets was observed for true ileal N digestibility between species. The inter-species correlation for true ileal digestibility was high for N (r 0.98 over 3 x 2 data; P = 0.11) and AA (r 0.87 over 26 x 2 data; P < 0.0001). Overall, this supports the use of the pig as a model for predicting differences among dietary protein digestibility, especially regarding true ileal N digestibility, in man.

Hydrolyzed dietary casein as compared with the intact protein reduces postprandial peripheral, but not whole-body, uptake of nitrogen in humans

BACKGROUNDnCompared with slow proteins, fast proteins are more completely extracted in the splanchnic bed but contribute less to peripheral protein accretion; however, the independent influence of absorption kinetics and the amino acid (AA) pattern of dietary protein on AA anabolism in individual tissues remains unknown.nnnOBJECTIVEnWe aimed to compare the postprandial regional utilization of proteins with similar AA profiles but different absorption kinetics by coupling clinical experiments with compartmental modeling.nnnDESIGNnExperimental data pertaining to the intestine, blood, and urine for dietary nitrogen kinetics after a 15N-labeled intact (IC) or hydrolyzed (HC) casein meal were obtained in parallel groups of healthy adults (n = 21) and were analyzed by using a 13-compartment model to predict the cascade of dietary nitrogen absorption and regional metabolism.nnnRESULTSnIC and HC elicited a similar whole-body postprandial retention of dietary nitrogen, but HC was associated with a faster rate of absorption than was IC, resulting in earlier and stronger hyperaminoacidemia and hyperinsulinemia. An enhancement of both catabolic (26%) and anabolic (37%) utilization of dietary nitrogen occurred in the splanchnic bed at the expense of its further peripheral availability, which reached 18% and 11% of ingested nitrogen 8 h after the IC and HC meals, respectively.nnnCONCLUSIONSnThe form of delivery of dietary AAs constituted an independent factor of modulation of their postprandial regional metabolism, with a fast supply favoring the splanchnic dietary nitrogen uptake over its peripheral anabolic use. These results question a possible effect of ingestion of protein hydrolysates on tissue nitrogen metabolism and accretion. This trial was registered at clinicaltrials.gov as NCT00873951.

Hydrolyzed casein influences intestinal mucin gene expression in the rat.

The effect of hydrolyzed casein (HC) on the expression of three mucin genes (Muc2, Muc3, and Muc4) in the rat intestine was investigated using quantitative real-time polymerase chain reaction. After a 10 day acclimatization period, rats received for 8 days the test diets containing either HC or a synthetic amino acid (SAA) mixture as the sole source of nitrogen or a protein-free (PF) diet (n = 12 per treatment). The addition of HC or the SAA mixture to the diet significantly improved average daily gain, average daily food intake, and gain:feed ratio as compared with the PF diet. Terminal ileal endogenous N flow was significantly higher for the HC-fed rats in comparison with either the SAA or the PF rats (p < or = 0.001). HC supported a significant increase of Muc3 mRNA (277 and 229% of that for diets PF and SAA, respectively; p < or = 0.05) in the small intestinal tissue and Muc4 mRNA (325 and 265% of that for diets PF and SAA, respectively; p < or = 0.05) in the colon. In conclusion, HC enhances ileal endogenous N flow and up-regulates in vivo the expression of some individual mucin genes.

Animal models for determining amino acid digestibility in humans – a review

Animal models have been commonly used for determining amino acid digestibility in humans. This allows digestibility assays to be undertaken more efficiently than those undertaken using humans directly. The laboratory rat, usually considered as a suitable animal model, has been widely used, especially as the rat is easy to raise and relatively inexpensive to house. Although more technically demanding, the pig has also been promoted as a useful model for human nutrition studies. It may be a better model than the rat, as it is a meal eater, its upper digestive tract is anatomically and physiologically closer to that of humans and it eats most foods consumed by humans. Amino acid digestibility may be determined either at the faecal or the ileal level, the latter being considered the most accurate. This contribution evaluates the suitability of the rat and pig as animal models for assessing ileal and faecal amino acid digestibility in humans. The drawbacks and advantages of using these animal models are discussed. The review is based mainly on results from controlled studies comparing both species; however, as the number of these studies is limited, data from indirect comparisons also provide insight.

Endogenous proteins in terminal ileal digesta of adult subjects fed a casein-based diet

BACKGROUNDnAlthough there are several published estimates of the endogenous amino acid composition of ileal digesta in humans, to our knowledge, there are no systematic studies of ileal digesta endogenous proteins.nnnOBJECTIVESnWe determined the nature and composition of endogenous nitrogen-containing substances lost from the upper digestive tract of humans.nnnDESIGNnDigesta were collected from the terminal ileum for a period of 8 h by using a nasoileal tube in 6 adult subjects fed a single meal that contained 22% of casein as the only source of nitrogen.nnnRESULTSnThe total nitrogen that passed the terminal ileum was 39.3 mg/g native digesta dry matter. Of this amount, 86% was proteinaceous, ~60% was bacterial protein, ~7% was soluble-free protein, ~15% was mucin protein, and ~5% was protein from intact mucosal cells. For nonprotein nitrogen, ~5% of the total nitrogen was ammonia, and ~4% of the total nitrogen was urea. Bacterial and human mucosal cellular DNA nitrogen were collectively ~0.5% of the total nitrogen. Approximately 30% of the nonprotein nitrogen (4% of the total nitrogen) remained unidentified. This amount was assumed to include free amino acids, RNAs, amines, and the tetrapyrroles bilirubin and biliverdin. Bacterial nitrogen, combined with ammonia and urea nitrogen, represented >68% of total ileal nitrogenous losses.nnnCONCLUSIONSnFindings are presented on the endogenous nitrogen-containing compounds that left the terminal ileum. Of particular significance is the observation that mucin was the most abundant truly endogenous component within the terminal ileal digesta. Bacterial protein, which was strictly nondietary rather than endogenous, contributed the highest proportion, by far, of nondietary protein, the result of which makes a significant contribution to published estimates of ileal endogenous amino acids and protein. The high concentration of bacterial protein and the presence of ammonia and urea nitrogen indicate potentially substantial microbial activity within the human distal small intestine.

A casein hydrolysate does not enhance ileal endogenous protein flows compared with the parent intact casein when fed to growing pigs

Abstract Background The form of dietary nitrogen (free peptides or intact proteins) may influence the amount of endogenous amino acids found at the terminal ileum of the pig, and it has been speculated that hydrolyzed dietary protein may lead to increased endogenous amino acids. Objective To compare the effect of dietary free peptides on ileal endogenous nitrogen and amino acid flows [ileal endogenous nitrogen flow (ENFL), ileal endogenous amino acid flow (EAAFL)] with that of peptides released naturally from dietary protein during digestion, from the same intact parent protein source. Methods Six pigs (mean body weight: 34 kg) were equipped with a postvalve T-caecum cannula. Semisynthetic test diets contained the same 15N-labeled intact casein (C) or hydrolyzed casein (HC). Pigs received the test diets every sixth day and the corresponding unlabeled diets in the intervening 5-d periods. Digesta were pooled from 4 to 10 h postprandially. EAAFL and ENFL, calculated with reference to the dietary marker titanium dioxide, were determined by isotope dilution for C and HC. Results Ileal EAAFL and ENFL (mean flows n = 5 of 1828 and 1912 μg/g of dry matter intake for diets HC and C, respectively) did not differ (P > 0.05) between pigs fed HC and C. Centrifugation and ultrafiltration of the HC digesta allowed an estimation of label recycling into gut endogenous proteins. Some 20% of ileal endogenous protein (diet HC, ultrafiltered digesta) was 15N-labeled due to tracer recycling. Conclusions The administration of a casein hydrolysate had no effect on ileal endogenous protein flows compared with C. There was no evidence of enhanced ileal endogenous protein losses with the HC diet.