The human intestinal epithelium is formed by a single layer of epithelial cells that separates the intestinal lumen from the underlying lamina propria. The space between these cells is sealed by tight junctions (TJ), which regulate the permeability of the intestinal barrier. TJ are complex protein structures comprised of transmembrane proteins, which interact with the actin cytoskeleton via plaque proteins. Signaling pathways involved in the assembly, disassembly, and maintenance of TJ are controlled by a number of signaling molecules, such as protein kinase C, mitogen-activated protein kinases, myosin light chain kinase, and Rho GTPases. The intestinal barrier is a complex environment exposed to many dietary components and many commensal bacteria. Studies have shown that the intestinal bacteria target various intracellular pathways, change the expression and distribution of TJ proteins, and thereby regulate intestinal barrier function. The presence of some commensal and probiotic strains leads to an increase in TJ proteins at the cell boundaries and in some cases prevents or reverses the adverse effects of pathogens. Various dietary components are also known to regulate epithelial permeability by modifying expression and localization of TJ proteins.

In this review, the terminology that is used to describe the bioavailability and ileal digestibility of AA in pig feed ingredients is defined. Aspects of the methodology to establish bioavailability and ileal digestibility values also are discussed, and recommendations about the use of these values are provided. Two main factors can contribute to differences between bioavailability and ileal digestibility of AA. First, some AA, such as Lys, may be absorbed in chemical complexes that preclude their use for metabolism. Second, fermentation in the upper gut may result in a net loss or gain of AA to the animal. In addition, dietary effects on the efficiency of using bioavailable AA intake for tissue growth or milk production should be considered and may be attributed to endogenous AA losses in the hindgut and the metabolic costs associated with endogenous gut protein synthesis and losses. Ileal digestibility values may be expressed as apparent ileal digestibility (AID), standardized ileal digestibility (SID), or true ileal digestibility (TID). These terms are used to specify how ileal endogenous AA losses are reflected in digestibility values. Ileal endogenous AA losses may be separated into basal losses, which are not influenced by feed ingredient composition, and specific losses, which are induced by feed ingredient characteristics such as levels and types of fiber and antinutritional factors. Values for AID are established when total ileal outflow of AA (i.e., the sum of endogenous losses and nondigested dietary AA) is related to dietary AA intake. A concern with the use of AID values is that these are not additive in mixtures of feed ingredients. This concern may be overcome by correcting AID values for defined basal endogenous losses of AA, which yields SID values. Furthermore, if the AID values are corrected for basal and specific endogenous losses, then values for TID are calculated. However, reliable procedures to routinely measure specific endogenous losses are not yet available. It is recommended that basal ileal endogenous losses of AA should be measured in digestibility experiments using a defined protein-free diet and that these losses are reported with observed AID and SID values. It is suggested that SID values should be used for feed formulation, at least until more information on TID values becomes available.

Untruncated PDCAAS values were generally higher than a DIAAS values, especially for the poorer quality proteins; therefore, the reported differences in the scores are of potential practical importance for populations in which dietary protein intake may be marginal.

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Lactobacillus species can exert health promoting effects in the gastrointestinal tract (GIT) through many mechanisms, which include pathogen inhibition, maintenance of microbial balance, immunomodulation, and enhancement of the epithelial barrier function. Different species of the genus Lactobacillus can evoke different responses in the host, and not all strains of the same species can be considered beneficial. Strain variations may be related to diversity of the cell surface architecture of lactobacilli and the bacteria's ability to express certain surface components or secrete specific compounds in response to the host environment. Lactobacilli are known to modify their surface structures in response to stress factors such as bile and low pH, and these adaptations may help their survival in the face of harsh environmental conditions encountered in the GIT. In recent years, multiple cell surface-associated molecules have been implicated in the adherence of lactobacilli to the GIT lining, immunomodulation, and protective effects on intestinal epithelial barrier function. Identification of the relevant bacterial ligands and their host receptors is imperative for a better understanding of the mechanisms through which lactobacilli exert their beneficial effects on human health.

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The aim of the study was to determine if there is a difference between ileal and faecal assays for determining amino acid and N digestibilities in adult human subjects. Comparison of true ileal amino acid and N digestibilities was also made between adult human subjects and growing pigs to establish the usefulness of the pig as a model animal. Five subjects with established ileostomies and six subjects with intact large bowels consumed a constant diet consisting of meat, vegetables, fruit, bread and dairy products for 7 d with collection of ileostomy contents or faeces respectively over the last 4 d. The study was repeated using 25 kg body weight ileostomized and intact pigs. Apparent amino acid and N digestibility coefficients were determined. For human subjects the faecal digestibility values were significantly higher (P < 0.05) than the ileal values for Arg, Asp, Gly, Phe, Pro, Ser, Thr and Trp. The faecal digestibility of Met was significantly lower than the ileal value. Determination of DNA, diaminopimelic acid (DAPA) and the digestibilities of pectin, hemicellulose and cellulose in human subjects indicated that some microbial colonization had occurred a t the terminal ileum after formation of an ileostomy; however, this was not as extensive as in the large intestine. True ileal amino acid and N digestibilities were calculated after correcting for the endogenous contribution of amino acids a t the terminal ileum determined using a protein-free diet. There were no significant differences between adult human subjects and pigs for true ileal dietary amino acid digestibility except for Thr, Phe, Cys and Met. There were no significant differences between adult humans and pigs for the ileal digestibility of dry matter and the faecal digestibility of gross energy.Amino acid digestibility: Pig: Man

For over 100 years it was believed that dietary protein must be completely hydrolysed before its constituent amino acids could be absorbed via specific amino acid transport systems. It is now known that the uptake of di- and tripeptides into the enterocyte is considerable, being transported across the intestinal endothelium by the PepT1 H+/peptide co-transporter. There is also evidence that some di- and tripeptides may survive cytosolic hydrolysis and be transported intact across the basolateral membrane. However, other than antigen sampling, the transport of larger intact macromolecules across the intestinal endothelium of the healthy adult human remains a controversial issue as there is little unequivocal in vivo evidence to support this postulation. The aim of the present review was to critically evaluate the scientific evidence that peptides/proteins are absorbed by healthy intestinal epithelia and pass intact into the hepatic portal system. The question of the absorption of oliogopeptides is paramount to the emerging science of food-derived bioactive peptides, their mode of action and physiological effects. Overall, we conclude that there is little unequivocal evidence that dietary bioactive peptides, other than di- and tripeptides, can cross the gut wall intact and enter the hepatic portal system in physiologically relevant concentrations.