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;n11) and growing pigs (mean body weight 40 kg;n15) 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 were¹⁵N-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 (r0·98 over 3 × 2 data;P = 0·11) and AA (r0·87 over 26 × 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.

It is important to be able to characterise foods and feedstuffs according to their available amino acid contents. This involves being able to determine amino acids chemically and the conduct of bioassays to determine amino acid digestibility and availability. The chemical analysis of amino acids is not straightforward and meticulousness is required to achieve consistent results. In particular and for accuracy, the effect of hydrolysis time needs to be accounted for. Some amino acids (for example, lysine) can undergo chemical modification during the processing and storage of foods, which interferes with amino acid analysis. Furthermore, the modified amino acids may also interfere with the determination of digestibility. A new approach to the determination of available lysine using a modifiedin vivodigestibility assay is discussed. Research is required into other amino acids susceptible to structural damage. There is recent compelling scientific evidence that bacterial activity in the small intestine of animals and man leads to the synthesis and uptake of dietary essential amino acids. This has implications for the accuracy of the ileal-based amino acid digestibility assay and further research is required to determine the extent of this synthesis, the source of nitrogenous material used for the synthesis and the degree of synthesis net of amino acid catabolism. Although there may be potential shortcomings in digestibility assays based on the determination of amino acids remaining undigested at the terminal ileum, there is abundant evidence in simple-stomached animals and growing evidence in human subjects that faecal-based amino acid digestibility coefficients are misleading. Hindgut microbial metabolism significantly alters the undigested dietary amino acid profile. The ileal amino acid digestibility bioassay is expected to be more accurate than its faecal-based counterpart, but correction of the ileal amino acid flow for amino acids of endogenous origin is necessary. Approaches to correcting for the endogenous component are discussed.

The intestinal epithelium of adult humans acts as a differentially permeable barrier that separates the potentially harmful contents of the lumen from the underlying tissues. Any dysfunction of this boundary layer that disturbs the homeostatic equilibrium between the internal and external environments may initiate and sustain a biochemical cascade that results in inflammation of the intestine. Key to such dysfunction are genetic, microbial and other environmental factors that, singularly or in combination, result in chronic inflammation that is symptomatic of inflammatory bowel disease (IBD). The aim of the present review is to assess the scientific evidence to support the hypothesis that defective transepithelial transport mechanisms and the heightened absorption of intact antigenic proinflammatory oligopeptides are important contributing factors in the pathogenesis of IBD.

Vitamins are essential components of enzyme systems involved in normal growth and function. The quantitative estimation of the proportion of dietary vitamins, that is in a form available for utilization by the human body, is limited and fragmentary. This review provides the current state of knowledge on the bioavailability of thirteen vitamins and choline, to evaluate whether there are differences in vitamin bioavailability when human foods are sourced from animals or plants. The bioavailability of naturally occurring choline, vitamin D, vitamin E, and vitamin K in food awaits further studies. Animal-sourced foods are the almost exclusive natural sources of dietary vitamin B-12 (65% bioavailable) and preformed vitamin A retinol (74% bioavailable), and contain highly bioavailable biotin (89%), folate (67%), niacin (67%), pantothenic acid (80%), riboflavin (61%), thiamin (82%), and vitamin B-6 (83%). Plant-based foods are the main natural sources of vitamin C (76% bioavailable), provitamin A carotenoid β-carotene (15.6% bioavailable), riboflavin (65% bioavailable), thiamin (81% bioavailable), and vitamin K (16.5% bioavailable). The overview of studies showed that in general, vitamins in foods originating from animals are more bioavailable than vitamins in foods sourced from plants.

The objective of the review is to revisit the findings of the 2011 Food and Agriculture Organization of the United Nations (FAO) Expert Consultation on Dietary Protein Quality Evaluation in Human Nutrition, and to report on progress on uptake of the findings. It is evident that since 2011 there has been a concerted research effort to enhance an understanding of the protein quality of foods. The validity of the growing pig ileal protein digestibility assay has been confirmed and numerous studies reported using the growing pig as a model to give true ileal amino acid digestibility values for foods as consumed by humans. This has allowed for the determination of digestible indispensable amino acid scores (DIAAS) for a range of foods. A new non-invasive true ileal amino acid digestibility assay in humans which can be applied in different physiological states, called the dual-isotope assay, has been developed and applied to determine the DIAAS values of foods. It is concluded that DIAAS is currently the most accurate score for routinely assessing the protein quality rating of single source proteins. In the future, the accuracy of DIAAS can be enhanced by improved information on: the ideal dietary amino acid balance including the ideal dispensable to indispensable amino acid ratio; dietary indispensable amino acid requirements; effects of processing on ileal amino acid digestibility and lysine bioavailability. There is a need to develop rapid, inexpensive in vitro digestibility assays. Conceptual issues relating DIAAS to food regulatory claims, and to holistic indices of food nutritional and health status are discussed. The first recommendation of the 2011 Consultation regarding treating each indispensable amino acid as an individual nutrient has received little attention. Consideration should be given to providing food label information on the digestible contents of specific indispensable amino acids.