High protein wheats for poultry. 1. Use in broiler diets

1971 ◽  
Vol 11 (53) ◽  
pp. 619 ◽  
Author(s):  
W Turner ◽  
GG Payne

High protein wheat was the sole cereal in 20 and 25 per cent crude protein broiler starter diets. On the. 25 per cent protein diet, performance was maximized without amino acid supplementation. Using high protein wheat in 20 per cent protein diets, growth rate was improved by l-lysine supplementation of 0.3 per cent. However, this growth rate was not at a maximum level. Some other dietary factor was necessary, and this did not appear to be essential amino acids, singly or in combination.

2016 ◽  
Vol 37 (3) ◽  
pp. 1539 ◽  
Author(s):  
Danilo Vargas Gonçalves Vieira ◽  
Thiago De Sousa Melo ◽  
José Humberto Vilar da Silva ◽  
Fernando Guilherme Perazzo Costa ◽  
Danilo Teixeira Cavalcante ◽  
...  

Three hundred and twenty-four DeKalb White laying hens aged 42 weeks were distributed in a completely randomised design with nine treatments and six replicates of six birds in each treatment. The experiment lasted 112 days. Diets were: T1 = 16.02% crude protein - CP [Met + Lys + Thr + Trp + Val]; T2 = 14.02% CP [Met + Lys + Thr + Trp + Ile + Val]; T3 = 14.02% CP [no amino acid supplementation]; T4 = 14.02% CP [Met + Lys + Thr + Trp]; T5 = 14.02% CP [Met + Lys + Thr]; T6 = 14.02% CP [Met]; T7 = 14.02% CP [Lys]; T8 = 14.02% CP [Thr]; T9 = 14.02% CP [Trp]. Regarding the quality of the eggs, the percentage of yolk and albumen, shell thickness and Haugh unit were not affected by the different diets. The percentage of shell, specific gravity and albumen height showed significant differences. We found that supplementation of only one amino acid in the diet (T7, T8 or T9), with the exception of methionine (T6), worsened performance relative to the control. Supplementation of three amino acids (methionine, lysine and threonine; T5) or four amino acids (methionine, lysine, threonine and tryptophan; T4) worsened egg production and conversion per mass and per dozen eggs; however, feed intake and egg weight and mass were similar to the control treatment. When all amino acids (methionine, lysine, threonine, tryptophan, isoleucine and valine; T2) were supplemented performance was similar to the control treatment in all variables. Supplementation of methionine, lysine and threonine is essential for birds in the laying phase; however the addition of six essential amino acids (lysine, methionine, threonine, tryptophan, valine and isoleucine) to the diet of laying hens is important for a good productive performance comparable with the control treatment T1. However, the inclusion of the latter two (isoleucine and valine) is justified only if the production cost is lower.


2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Sonia Yun Liu ◽  
Shemil P. Macelline ◽  
Peter V. Chrystal ◽  
Peter H. Selle

AbstractThe prime purpose of this review is to explore the pathways whereby progress towards reduced-crude protein (CP) diets and sustainable chicken-meat production may be best achieved. Reduced-CP broiler diets have the potential to attenuate environmental pollution from nitrogen and ammonia emissions; moreover, they have the capacity to diminish the global chicken-meat industry’s dependence on soybean meal to tangible extents. The variable impacts of reduced-CP broiler diets on apparent amino acid digestibility coefficients are addressed. The more accurate identification of amino acid requirements for broiler chickens offered reduced-CP diets is essential as this would diminish amino acid imbalances and the deamination of surplus amino acids. Deamination of amino acids increases the synthesis and excretion of uric acid for which there is a requirement for glycine, this emphasises the value of so-called “non-essential” amino acids. Starch digestive dynamics and their possible impact of glucose on pancreatic secretions of insulin are discussed, although the functions of insulin in avian species require clarification. Maize is probably a superior feed grain to wheat as the basis of reduced-CP diets; if so, the identification of the underlying reasons for this difference should be instructive. Moderating increases in starch concentrations and condensing dietary starch:protein ratios in reduced-CP diets may prove to be advantageous as expanding ratios appear to be aligned to inferior broiler performance. Threonine is specifically examined because elevated free threonine plasma concentrations in birds offered reduced-CP diets may be indicative of compromised performance. If progress in these directions can be realised, then the prospects of reduced-CP diets contributing to sustainable chicken-meat production are promising.


1993 ◽  
Vol 264 (6) ◽  
pp. G1057-G1065 ◽  
Author(s):  
C. Moundras ◽  
C. Remesy ◽  
C. Demigne

The aim of the present study was to evaluate the effect of changes in dietary protein level on overall availability of amino acids for tissues. For this purpose, rats were adapted to diets containing various concentrations of casein (7.5, 15, 30, and 60%) and were sampled either during the postprandial or postabsorptive period. In rats fed the protein-deficient diet, glucogenic amino acids (except threonine) tended to accumulate in plasma, liver, and muscles. In rats fed high-protein diets, the hepatic balance of glucogenic amino acids was markedly enhanced and their liver concentrations were consistently depressed. This response was the result of a marked induction of amino acid catabolism (a 45-fold increase of liver threonine-serine dehydratase activity was observed with the 60% casein diet). The muscle concentrations of threonine, serine, and glycine underwent changes parallel to plasma and liver concentrations, and a significant reduction of glutamine was observed. During the postabsorptive period, adaptation to high-protein diets resulted in a sustained catabolism of most glucogenic amino acids, which accentuated the drop in their concentrations (especially threonine) in all the compartments studied. The time course of metabolic adaptation from a 60 to a 15% casein diet has also been investigated. Adaptation of alanine and glutamine metabolism was rapid, whereas that of threonine, serine, and glycine was delayed and required 7-11 days. This was paralleled by a relatively slow decay of liver threonine-serine dehydratase (T-SDH) activity in contrast to the rapid adaptation of pyruvate kinase activity after refeeding a high-carbohydrate diet.(ABSTRACT TRUNCATED AT 250 WORDS)


1967 ◽  
Vol 168 (1013) ◽  
pp. 421-438 ◽  

The uptake of thirteen essential amino acids by mouse LS cells in suspension culture was determined by bacteriological assay methods. Chemostat continuous-flow cultures were used to determine the effect of different cell growth rates on the quantitative amino acid requirements for growth. The growth yields of the cells ( Y = g cell dry weight produced/g amino acid utilized) were calculated for each of the essential amino acids. A mixture of the non-essential amino acids, serine, alanine and glycine increased the cell yield from the essential amino acids. The growth yields from nearly all the essential amino acids in batch culture were increased when glutamic acid was substituted for the glutamine in the medium. The growth yields from the amino acids in batch culture were much less at the beginning than at the end of the culture. The highest efficiencies of conversion of amino acids to cell material were obtained by chemostat culture. When glutamic acid largely replaced the glutamine in the medium the conversion of amino acid nitrogen to cell nitrogen was 100 % efficient (that is, the theoretical yield was obtained) at the optimum growth rate (cell doubling time, 43 h). The maximum population density a given amino acid mixture will support can be calculated from the data. It is concluded that in several routinely used tissue culture media the cell growth is limited by the amino acid supply. In batch culture glutamine was wasted by (1) its spontaneous decomposition to pyrrolidone carboxylic acid and ammonia, and (2) its enzymic breakdown to glutamic acid and ammonia, but also glutamine was used less efficiently than glutamic acid. Study of the influence of cell growth rate on amino acid uptake rates per unit mass of cells indicated that a marked change in amino acid metabolism occurred at a specific growth rate of 0.4 day -1 (cell doubling time, 43 h). With decrease in specific growth rate below 0.4 day -1 there was a marked stimulation of amino acid uptake rate per cell and essential amino acids were consumed increasingly for functions other than synthesis of cell material.


2002 ◽  
Vol 25 (4) ◽  
pp. 261-268 ◽  
Author(s):  
R. Bellomo ◽  
H. K. Tan ◽  
S. Bhonagiri ◽  
I. Gopal ◽  
J. Seacombe ◽  
...  

Aims To study the effect of combined continuous veno-venous hemodiafiltration (CVVHDF) and high (2.5 g/kg/day) parenteral amino acid supplementation on nitrogen balance, amino acid losses and azotemic control in a cohort of patients with severe acute renal failure (ARF). Methods We administered 2.5 grams/kg/day of amino acids intravenously to seven critically ill patients with ARF. We obtained paired blood and ultrafiltrate (UF) samples (n=20) and calculated amino acid clearances and losses, nitrogen balance, protein catabolic rate and total nitrogen losses. Results The median total serum amino acid concentration was high at 5.2 mmol/L with particularly high concentrations of ornithine, lysine, and phenylalanine, but a low level of histidine. The median overall amino acid clearance was 18.6 ml/min (range: 12 to 29 ml/min). UF losses as percentage of administered dose were high for tyrosine (53.6 %) but low for methionine (3.0 %) and arginine (2.3 %). A positive nitrogen balance was achieved in 7 (35%) of the 20 study days with an overall median nitrogen balance of -1.8 g/day. Urea levels were maintained at a median of 26.6 mmol/L. Conclusions High protein intake increases the serum concentrations of most amino acids. Such protein supplementation, when coupled with CVVHDF, achieves a slightly negative overall nitrogen balance in extremely catabolic patients while still allowing adequate azotemic control.


2020 ◽  
Vol 78 (Supplement_3) ◽  
pp. 79-85
Author(s):  
Kenji Nagao ◽  
Takeshi Kimura

Abstract This paper reviews developments regarding the use of plasma-free amino acid (PFAA) profiles as biomarkers for detecting and predicting disease risk. This work was initiated and first published in 2006 and was subsequently developed by Ajinomoto Co., Inc. After commercialization in 2011, PFAA-based tests were adopted in over 1500 clinics and hospitals in Japan, and numerous clinician-led studies have been performed to validate these tests. Evidence is accumulating that PFAA profiles can be used for diabetes prediction and evaluation of frailty; in particular, decreased plasma essential amino acids could contribute to the pathophysiology of severe frailty. Integration of PFAA evaluation as a biomarker and effective essential amino acid supplementation, which improves physical and mental functions in the elderly, could facilitate the development of precision nutrition, including personalized solutions. This present review provides the background for the technology as well as more recent clinical findings, and offers future possibilities regarding the implementation of precision nutrition.


1986 ◽  
Vol 55 (3) ◽  
pp. 659-668 ◽  
Author(s):  
Ronald O. Ball ◽  
James L. Atkinson ◽  
Henry S. Bayley

1. The catabolism of L-[ l-14C]phenylalanine was used to indicate the effects of single amino acid supplementation of an inadequate protein diet (200 g crude protein (nitrogen x 6.25)/kg) on the utilization of dietary amino acids in pigs of 2.5 kg body-weight reared on an adequate protein diet (240 g crude protein/kg) containing skim milk and a mixture of free amino acids.2. The oxidation of phenylalanine was decreased by the addition of proline or arginine to the inadequate protein diet but not by the addition of threonine, methionine, lysine or a mixture of essential amino acids, indicating that proline and arginine were limiting the utilization of dietary amino acids in the inadequate protein diet.3. Dietary proline concentrations of 13.9 and 14.2 g/kg minimized phenylalanine oxidation in diets containing 200 or 260 g protein/kg. This indicates a dietary proline requirement of 14 g/kg.4. Increasing the dietary arginine concentration in a diet containing 240 g protein/kg showed that an arginine concentration of 5.1 g/kg minimized phenylalanine oxidation. However, increasing the arginine concentration in a diet containing 200 g protein/kg increased phenylalanine oxidation, suggesting an amino acid imbalance involving arginine at this lower level of protein.


2012 ◽  
Vol 108 (S2) ◽  
pp. S333-S336 ◽  
Author(s):  
Gertjan Schaafsma

PDCAAS is a widely used assay for evaluating protein quality. It is a chemical score, which is derived from the ratio between the first limiting amino acid in a test protein and the corresponding amino acid in a reference amino acid pattern and corrected for true faecal N digestibility. Chemical scores exceeding 100 % are truncated to 100 %. The advantages of the PDCAAS are its simplicity and direct relationship to human protein requirements. The limitations are as follows: the reference pattern is based on the minimum amino acid requirements for tissue growth and maintenance and does not necessarily reflect the optimum intake. Truncated PDCAAS of high-quality proteins do not give any information about the power of these proteins to compensate, as a supplement, for low levels of dietary essential amino acids in low-quality proteins. It is likely that faecal N digestibility does not take into account the loss from the colon of indispensable amino acids that were not absorbed in the ileum. Anti-nutritional factors, such as lectins and trypsin inhibitors, in several plant protein sources can cause heightened endogenous losses of amino acids, an issue which is particularly relevant in animal feedstuffs. The assumption that amino acid supplementation can completely restore biological efficiency of the protein source is incorrect since the kinetics of digestion and absorption between supplemented free amino acids and amino acids present in dietary proteins, are different.


2009 ◽  
pp. 101-107
Author(s):  
Zoltán Mezei ◽  
Ágnes Pongrácznl Barancsi ◽  
Péter Sipos ◽  
Zoltán Győri ◽  
János Csapó

We analysed the crude protein content, amino acid content, amino acid composition of four forage and milling III. quality winter wheat varieties (Magor, Hunor, Róna and Kondor) from their samples from five following years (2003, 2004, 2005, 2006, 2007). We found that quantity of essential and non-essential amino acids rose with increase in crude protein content. On examination of protein amino acid composition in relation to crude protein content we found that the crude protein content increased the quantities of the non-essential amino acids also rose, while those of the essential amino acids decreased as the lysine, the limiting amino acid of wheat. We also established that, as crude protein content increased, the biological value of the protein decreased.


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