Many improvements have been made to bring infant formula (IF) closer to human milk (HM) regarding its nutritional and biological properties. Nevertheless, the protein components of HM and IF are still different, which may affect their digestibility. This study aimed to evaluate and compare the protein digestibility of HM and IF using the infant INFOGEST digestion method. Pooled HM and a commercial IF were subjected to the infant INFOGEST method, which simulates the physiological digestion conditions of infants, with multiple directions, i.e. the curd state, gel images of SDS-PAGE, molecular weight distribution, free amino acid concentrations and in vitro protein digestion rate. HM underwent proteolysis before digestion and tended to have a higher protein digestion rate with finer curds during gastric digestion, than the IF. However, multifaceted analyses showed that the protein digestibility of HM and IF was not significantly different after gastrointestinal digestion. In conclusion, the infant INFOGEST method showed that the digestibility of HM and IF proteins differed to some extent before digestion and after gastric digestion, but not at the end of gastrointestinal digestion. The findings of this study will contribute to the refinement of IF with better protein digestibility in infant stomach.

During industrial processing, heat treatments applied to infant formulas may affect protein digestion. Recently, innovative processing routes have been developed to produce minimally heat-processed infant formula. Our objective was to compare the in vivo protein digestion kinetics and protein quality of a minimally processed (T−) and a heat-treated (T+++) infant formula. Sixty-eight male Wistar rats (21 d) were fed with either a diet containing 40 % T− (n 30) or T+++ (n 30), or a milk protein control diet (n 8) during 2 weeks. T− and T+++ rats were then sequentially euthanised 0, 1, 2, 3 or 6 h (n 6/time point) after ingestion of a meal containing their experimental diet. Control rats were euthanised 6 h after ingestion of a protein-free meal to determine nitrogen and amino acid endogenous losses. Nitrogen and amino acid true caecal digestibility was high for both T− and T+++ diets (> 90 %), but a tendency towards higher nitrogen digestibility was observed for the T− diet (96·6 ± 3·1 %) compared with the T+++ diet (91·9 ± 5·4 %, P = 0·0891). This slightly increased digestibility led to a greater increase in total amino acid concentration in plasma after ingestion of the T− diet (P = 0·0010). Comparable protein quality between the two infant formulas was found with a digestible indispensable amino acid score of 0·8. In conclusion, this study showed that minimal processing routes to produce native infant formula do not modify protein quality but tend to enhance its true nitrogen digestibility and increase postprandial plasma amino acid kinetics in rats.

The rat model can be used to assess ileal protein digestibility rapidly and in first intention, but no standardised method exists. Our objective was to compare methods to assess protein digestibility, depending on collection site (ileum/caecum) and use of a non-absorbable marker. A meal containing either casein, gluten or pea protein and chromium oxide as non-absorbable marker was given to male Wistar rats and the entire digestive content was collected 6 h later. Total chromium recovery was incomplete and variable, depending on protein source. We observed no significant difference in digestibility between the methods for any of the protein sources tested. Although none of the methods tested is optimal, our results suggest that caecal digestibility can be used as a proxy of ileal digestibility in rats without using a non-absorbable marker. This simple method makes it possible to evaluate protein digestibility of new alternative protein sources for human consumption.

The objective of this study was to assess the nutritional quality of pea protein isolate in rats and to evaluate the impact of methionine (Met) supplementation. Several protein diets were studied: pea protein, casein, gluten, pea protein–gluten combination and pea protein supplemented with Met. Study 1: Young male Wistar rats (n 8/group) were fed the test diets ad libitum for 28 d. The protein efficiency ratio (PER) was measured. Study 2: Adult male Wistar rats (n 9/group) were fed the test diets for 10 d. A protein-free diet group was used to determine endogenous losses of N. The rats were placed in metabolism cages for 3 d to assess N balance, true faecal N digestibility and to calculate the Protein Digestible-Corrected Amino Acid Score (PDCAAS). They were then given a calibrated meal and euthanised 6 h later for collection of digestive contents. The true caecal amino acid (AA) digestibility was determined, and the Digestible Indispensable Amino Acid Score (DIAAS) was calculated. Met supplementation increased the PER of pea protein (2·52 v. 1·14, P < 0·001) up to the PER of casein (2·55). Mean true caecal AA digestibility was 94 % for pea protein. The DIAAS was 0·88 for pea protein and 1·10 with Met supplementation, 1·29 for casein and 0·25 for gluten. Pea protein was highly digestible in rats under our experimental conditions, and Met supplementation enabled generation of a mixture that had a protein quality that was not different from that of casein.

Protein structure influences the accessibility of enzymes for digestion. The proportion of intramolecular β-sheets in the secondary structure of native proteins has been related to a decrease in protein digestibility. Changes to proteins that can be considered positive (for example, denaturation and random coil formation) or negative (for example, aggregation and Maillard reactions) for protein digestibility can occur simultaneously during processing. The final result of these changes on digestibility seems to be a counterbalance of the occurrence of each phenomenon. Occurrence of each phenomenon depends on the conditions applied, but also on the source and type of the protein that is processed. The correlation between denaturation enthalpy after processing and protein digestibility seems to be dependent on the protein source. Heat seems to be the processing parameter with the largest influence on changes in the structure of proteins. The effect of moisture is usually limited to the simultaneous application of heat, but increasing level of moisture during processing usually increases structural changes in proteins. The effect of shear on protein structure is commonly studied using extrusion, although the multifactorial essence of this technology does not allow disentanglement of the separate effects of each processing parameter (for example, heat, shear, moisture). Although most of the available literature on the processing of feed ingredients reports effects on protein digestibility, the mechanisms that explain these effects are usually lacking. Clarifying these mechanisms could aid in the prediction of the nutritional consequences of processing conditions.

The subject of protein quality assessment of foods and diets was addressed at the Codex Committee on Vegetable Proteins (1982–1989), FAO/WHO (1989, 2001) and WHO/FAO (2002) expert reviews. These international developments are summarized in this manuscript. In 1989, a Joint FAO/WHO Expert Consultation on Protein Quality Evaluation reviewed knowledge of protein quality assessment of foods, and specifically evaluated amino acid score corrected for protein digestibility, the method recommended by the Codex Committee on Vegetable Proteins. The report of the Consultation published in 1991 concluded that the Protein Digestibility-corrected Amino Acid Score (PDCAAS) method was the most suitable approach for routine evaluation of protein quality for humans. The Consultation recognized that the amino acid scoring pattern proposed by FAO/WHO/UNU (1985) for preschool children was at that time the most suitable pattern for calculating PDCAAS for all ages except infants in which case the amino acid composition of human milk was recommended to be the basis of the scoring pattern. The rat balance method was considered as the most suitable practical method for predicting protein digestibility by humans. Since its adoption by FAO/WHO (1991), the PDCAAS method has been criticised for a number of reasons. The FAO/WHO (2001) Working Group on analytical issues related to protein quality assessed the validity of criticisms of the PDCAAS method. While recognizing a distinct regulatory use of protein quality data, the Working Group recommended that the PDCAAS method may be inappropriate for the routine prediction of protein quality of novel and sole source foods which contain high levels of anti nutritional factors; and that for regulatory purposes, the method should be revised to permit values of >100 for high quality proteins. In evaluating the recommendations of the Working Group, the WHO/FAO (2002) Expert Consultation on Protein and Amino Acid Requirements endorsed the PDCAAS method with minor modifications to the calculation method but also raised several issues. These included the calculation of scoring patterns; prediction of amino acid digestibility by faecal and ileal methods; reduced bioavailability of lysine in processed proteins; truncation of the amino acid score and consequent PDCAAS value; protein digestibility as a first limiting factor in determining the overall available dietary nitrogen; and the calculation of amino acid score for a dietary protein mixture. These concerns were considered particularly important in relation to the regulatory aspects of protein quality of foods, and their resolution was urgently recommended through a new separate expert review.

Forty Menz rams weighing 20 to 22 kg and aged 13 to 18 months were individually offered 1·0 kg/day chopped maize stover and one of five supplements over a 70-day growth trial followed by a 10-day metabolism trial. The amounts of supplement offered were designed to supply 4·4 g nitrogen per day and with stover, sufficient nutrients to allow growth rates of 50 g/day. The control supplement, 80 g dry matter (DM) per day extracted noug (Guizotia abyssinica) meal, was compared with 194 to 212 g DM per day of fruits (pods (carpels) with seeds) of Acacia tortilis, A. albida, A. nilotica and A. sieberiana. For the control and four Acacia supplements respectively, mean growth rates were 32, 32, 21, 16, 4 (s.e.6) g/day and mean stover intakes 483, 430, 401, 347, 320 (s.e. 74) g DM per day. The low growth rates and intakes with A. sieberiana and to a lesser extent A. nilotica were probably related to their content of phenolic compounds including insoluble proanthocyanidins which may have lowered the digestibility of neutral-detergent fibre and nitrogen. A. tortilis and A. albida would appear to be of comparable nutritive value to noug meal as supplements to maize stover. Unlike noug meal Acacia fruits are widely available in rural areas of Africa. Further research is required to identify other tree species suitable for use as supplements and how to overcome the anti-nutritional factors.

Adult male rabbits were fed on semi-purified diets containing soya-bean protein isolate, casein or formaldehyde-treated casein as the protein source and 1 g cholesterol and 5 g of the non-absorbable marker chromic oxide/kg diet. The concentration of cholesterol in serum and in liver was increased on both the casein and formaldehyde-treated-casein diets. Excretion of bile acids and their concentration in faeces were lower in rabbits fed on casein or formaldehyde-treated casein when compared with rabbits fed on soya-bean protein. Apparent digestibility of nitrogen was lowest when formaldehyde-treated casein was fed, and highest on the casein diet. In rabbits fed on casein treated with formaldehyde, higher proportions of N were found in the water-soluble and trichloroacetic acid-insoluble protein fractions of the gastrointestinal tract contents compared with rabbits on the other two diets. Absorption of phosphate from the gastrointestinal tract was higher in rabbits fed on casein than in rabbits fed on soya-bean protein or formaldehyde-treated casein. The results indicate that, in rabbits, protein digestibility may not be an important determinant of serum cholesterol.