Endogenous amino acid flow in the avian ileum: quantification using three techniques.

The aim of the present study was to compare the protein-free diet, guanidinated casein (GuC) and enzyme hydrolysed casein (EHC) methods for the quantification of endogenous amino acid (AA) flow in the avian ileum. Growing broiler chickens (5 weeks old) were used. All three assay diets were based on dextrose, and in the GuC and EHC diets GuC or EHC were the sole source of N. Endogenous AA flows determined with the use of protein-free diet were considerably lower (P<0.05) than those determined by the GuC and EHC methods. The total endogenous AA flows determined by the GuC and EHC methods were almost 3-fold greater (P<0.05) than those determined by the protein-free diet. The endogenous AA values obtained from GuC and EHC methods were similar (P>0.05), except for the flow of arginine, which was lower (P<0.05) in the EHC method. Glutamic acid, aspartic acid, threonine and glycine were the predominant endogenous AA present in digesta from the distal ileum. The contents of methionine, histidine and cystine were lower compared with other AA. The method of determination had no effect on the AA composition of endogenous protein, except for threonine, glutamic acid, lysine, arginine and cystine. The concentrations of threonine and arginine were lower (P<0.05) and that of lysine was higher (P<0.05) with the EHC method compared with the other two methods. The concentration of glutamic acid was greater (P<0.05) and that of cystine was lower (P<0.05) in the EHC and GuC methods compared with the protein-free diet method. The results showed that the ileal endogenous flows of N and AA are markedly enhanced by the presence of protein and peptides, above those determined following feeding of a protein-free diet. It is concluded that the use of EHC and GuC methods enables the measurement of ileal endogenous losses in chickens under normal physiological conditions.

A comparison of ileal digesta and excreta analysis for the determination of amino acid digestibility in food ingredients for poultry.

1. The apparent ileal and excreta digestibilities of amino acids in 15 samples representing 12 food ingredients were determined using 5-week-old male broiler chickens. The ingredients included 3 samples of cereals (wheat, maize and sorghum), 6 samples of plant protein meals (soyabean meal, cottonseed meal, canola meal and sunflower meal) and 6 samples of animal protein meals (meat meal, meat-and-bone meal, feather meal and fish meal). 2. The test ingredients were incorporated as the sole source of dietary protein in assay diets. Each diet was offered ad libitum to 3 pens (4 birds/pen) from d 35 to d 42 post-hatching. Total collection of excreta was carried out during the last 4 d. All birds were killed on d 42 and the contents of the lower half of the ileum were collected. Apparent ileal and excreta amino acid digestibilities were calculated using acid-insoluble ash as the indigestible marker. 3. The influence of site of measurement was found to vary among food ingredients, among samples within an ingredient and among different amino acids within an ingredient. Ileal amino acid digestibility values were similar in some ingredients, but significantly lower or higher in others than the corresponding excreta values. 4. Average ileal and excreta amino acid digestibilities in sorghum and maize were similar, but significant differences were observed for individual amino acids. In contrast, ileal amino acid digestibility values were higher than the corresponding excreta digestibility values in wheat. 5. The average ileal and excreta digestibilites of amino acids in the 3 soyabean meal samples were similar although small, but significant differences were noted for individual amino acids. Site of measurement had no effect on the digestibility of amino acids in canola meal. Digestibilities of valine, isoleucine, phenylalanine, histidine, glutamic acid, alanine and tyrosine in sunflower meal and those of valine, methionine, isoleucine, leucine, lysine, glutamic acid and alanine in cottonseed meal were lower by excreta analysis. 6. Digestibilities in animal protein meals, with the exception of blood meal and fish meal, were consistently higher by excreta analysis. Ileal-excreta differences in individual amino acid digestibilities were more evident in feather meal, meat meal and meat-and-bone meal. 7. Threonine and valine were the indispensable amino acids that were more frequently influenced by the site of measurement. Of the dispensable amino acids, aspartic acid, serine, glutamic acid and alanine were the most affected. 8. Differences determined between ileal and excreta digestibilities in the present study clearly demonstrate that amino acid metabolism by hindgut microflora in chickens may be substantial and that digestibilities measured in the terminal ileum are more accurate measures of amino acid availability than those measured in the excreta.

Influence of guanidination on apparent ileal amino acid digestibility in some protein sources for broilers.

High pH employed during the guanidination process (conversion of lysine residues to homoarginine) and its possible effects on racemization of amino acid residues to D-forms and on amino acid digestibility are concerns often raised with the use of guanidinated proteins to estimate endogenous amino acid losses in monogastric animals. The objective of the present study was to investigate the influence of guanidination on apparent ileal amino acid digestibility of casein, soybean meal, cottonseed meal, and canola meal for broiler chickens. Apparent ileal digestibility of amino acids in guanidinated and unreacted proteins, with few exceptions, were found to be remarkably similar. These results suggest that the guanidination process has no influence on the susceptibility of proteins to proteolysis and that racemization is not a practical problem when the proteins are guanidinated at low temperatures.