The current recommendation, when calculating a protein digestibility-corrected amino acid score, is to determine the digestibility of a dietary protein across the entire digestive tract, using the rat as a model animal for humans. This fecal digestibility value is subsequently corrected for endogenous contributions of protein using a metabolic nitrogen value determined by feeding rats a protein-free diet. The limitations inherent with this method are well recognized, however, and determining the digestibility of a dietary protein to the end of the small intestine is the preferred alternative. Unlike the fecal digestibility assay, which has only one basic methodology, ileal digestibility values can be determined in a number of ways. We discuss the various methods available for determining ileal digestibility values and compare results obtained for dietary proteins using both fecal and ileal digestibility assays. The relative value of using individual amino acid digestibility values as opposed to nitrogen digestibility values is reviewed. In addition, we address issues surrounding measurement of endogenous nitrogen flows, and in particular, the relative merits of determining "true" versus "real" digestibility values.
Human milk was collected from women in their 10th-14th weeks of lactation, and was analysed for amino acids. Corrections were made for losses of amino acids which were presumed to occur during acid hydrolysis, using a non-linear mathematical model that describes the simultaneous processes of amino acid yield and decay. The mean amino acid composition of the human milk was found to be similar to previously reported estimates, although the cysteine content of the human milk in the present study was 20 % higher than the average literature estimate. True (corrected for endogenous amino acid excretions) ileal amino acid digestibility of human milk was determined using the 3-week-old piglet as a model animal for the human infant. The piglets were given either human milk (n 6) or a protein-free diet (n 6) for a 6 d experimental period. Cr 2 O 3 was added as an indigestible marker, to both the human milk and protein-free diet. At the end of the experimental period the piglets were anaesthetized and samples of digesta removed from the terminal ileum of each piglet. After sampling the piglets were killed. Endogenous ileal excretions of amino acids were determined in piglets fed on the protein-free diet. The true digestibilities of total N and amino acid N were 88 % and 95 % respectively. The true ileal digestibility of the non-amino acid N fraction in human milk, when calculated by difference was only 50 %. The true digestibility of the amino acids in human milk ranged from 81-101 % with threonine (86 %) being the least digestible essential amino acid. When the true ileal digestibility values were used to correct the amino acid composition of human milk, the pattern of digestible amino acids in human milk was different compared with the currently recommended pattern of amino acid requirements for the infant.
Determining the amino acid content of a protein involves the hydrolysis of that protein, usually in acid, until the protein-bound amino acids are released and made available for detection. Both the variability in the ease of peptide bond cleavage and differences in the acid stability of certain amino acids can significantly affect determination of a protein's amino acid content. By using multiple hydrolysis intervals, a greater degree of accuracy can be obtained in amino acid analysis. Correction factors derived by linear extrapolation of serial hydrolysis data are currently used. Compartmental modeling of the simultaneous hydrolysis (yield) and degradation (decay) of amino acids by nonlinear multiple regression of serial hydrolysis data has also been validated and applied to determine the amino acid composition of various biological samples, including egg-white lysozyme, human milk protein, and hair. Implicit in the routine application of serial hydrolysis in amino acid analysis, however, is an understanding that correction factors, derived either linearly or through the more accurate nonlinear multiple regression approach, need to be determined for individual proteins rather than be applied uniformly across all protein types.
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