scholarly journals The Dynamic Conversion of Dietary Protein and Amino Acids into Chicken-Meat Protein

Animals ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 2288
Author(s):  
Shemil P. Macelline ◽  
Peter V. Chrystal ◽  
Sonia Y. Liu ◽  
Peter H. Selle
Keyword(s):  
Amino Acids ◽  
Dietary Protein ◽  
Animal Species ◽  
Chicken Meat ◽  
Meat Industry ◽  
Protein Deposition ◽  
Meat Protein ◽  
Energy Needs ◽  
Gut Mucosa ◽  
Reduced Crude Protein

This review considers the conversion of dietary protein and amino acids into chicken-meat protein and seeks to identify strategies whereby this transition may be enhanced. Viable alternatives to soybean meal would be advantageous but the increasing availability of non-bound amino acids is providing the opportunity to develop reduced-crude protein (CP) diets, to promote the sustainability of the chicken-meat industry and is the focus of this review. Digestion of protein and intestinal uptakes of amino acids is critical to broiler growth performance. However, the transition of amino acids across enterocytes of the gut mucosa is complicated by their entry into either anabolic or catabolic pathways, which reduces their post-enteral availability. Both amino acids and glucose are catabolised in enterocytes to meet the energy needs of the gut. Therefore, starch and protein digestive dynamics and the possible manipulation of this ‘catabolic ratio’ assume importance. Finally, net deposition of protein in skeletal muscle is governed by the synchronised availability of amino acids and glucose at sites of protein deposition. There is a real need for more fundamental and applied research targeting areas where our knowledge is lacking relative to other animal species to enhance the conversion of dietary protein and amino acids into chicken-meat protein.

scholarly journals Progress towards reduced-crude protein diets for broiler chickens and sustainable chicken-meat production

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Sonia Yun Liu ◽  
Shemil P. Macelline ◽  
Peter V. Chrystal ◽  
Peter H. Selle
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Broiler Chickens ◽  
Crude Protein ◽  
Plasma Concentrations ◽  
Essential Amino Acids ◽  
Chicken Meat ◽  
Meat Production ◽  
Accurate Identification ◽  
Reduced Crude Protein

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.

The tissue and dietary protein and amino acid requirements of pigs from 8.0 to 20.0 kg live weight

1988 ◽  
Vol 46 (2) ◽  
pp. 283-290 ◽  
Author(s):  
R. G. Campbell ◽  
M. R. Taverner ◽  
C. J. Rayner
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Dietary Protein ◽  
Protein Concentration ◽  
Live Weight ◽  
Body Protein ◽  
Digestible Energy ◽  
Protein Deposition ◽  
Amino Acid Requirements ◽  
Ideal Protein

AbstractForty-three entire males were used to determine the pig's tissue requirements for protein and amino acids from 8·0 to 20·0 kg, and provide information on the capacity of diets formulated with conventional ingredients to contain the same levels and balances of amino acids as ideal protein to supply these nutrients. Seven diets with similar digestible energy (15·9 MJ digestible energy (DE) per kg) and crude protein concentrations from 119 to 232 g/kg (8·7 to 17·3 g lysine per kg) were offered ad libitum between 8·0 and 200 kg live weight. The rate of protein deposition was determined by comparative slaughter. The composition of the protein deposited in the whole empty body was determined from amino acid analyses of pigs killed at 8·0 kg and from the two extreme dietary treatments at 20·0 kg. Growth performance and the rates at which protein and lysine were deposited in the empty body increased linearly with increasing dietary protein concentration up to 187 g/kg and remained relatively constant thereafter. The corresponding dietary protein and lysine intakes required to support maximal protein accretion were 178 g/day (11·7 g/MJ DE) and 13·0 g/day (0·84 g/MJ DE) respectively. Based on the maximal deposition rates for protein (91·8 g/day), and lysine (5·96 g/day) and endogenous protein loss (77middot;6 g/day) estimated from the linear component of the relationship determined between protein deposition and apparent digestible protein intake, the pig's tissue requirements for protein and lysine were only 99·4 g/day (6·5 g/MJ DE) and 6·46 g/day (0·43 g/MJ DE) respectively. This disparity between the pig's tissue protein and amino acid requirements and the dietary levels needed to support these was associated with the fact that the apparent digestibility and biological value of the dietary protein were 0·92 and 0·602 respectively. Apart from small differences in the lysine content of body protein and the methionine: lysine ratio, the average amino acid composition of pigs killed at 8·0 kg, and from the diet of highest protein concentration at 20 kg, was similar to that of ideal protein, indicating that the low utilizability of dietary protein for tissue growth and maintenance was probably associated with low amino acid digestibility and/or availability. The implications of the results with respect to expression of the growing pig's requirements for protein and amino acids are discussed.

Regulatory signals for intestinal amino acid transporters and peptidases

1988 ◽  
Vol 255 (2) ◽  
pp. G151-G157 ◽  
Author(s):  
R. P. Ferraris ◽  
W. W. Kwan ◽  
J. Diamond
Keyword(s):  
Amino Acids ◽  
Brush Border ◽  
Dietary Protein ◽  
Animal Species ◽  
Amino Acid Transporters ◽  
Protein Digestion ◽  
Uptake Rates ◽  
Regulatory Signal ◽  
Pancreatic Proteases ◽  
Peptide Uptake

Dietary protein ultimately regulates many processes involved in protein digestion, but it is often unclear whether proteins themselves, peptides, or amino acids (AAs) are the proximate regulatory signal. Hence we compared several processes involved in protein digestion in mice adapted to one of three rations, identical except for containing 54% of either casein, a partial hydrolysate of casein, or a free AA mixture simulating a complete hydrolysate of casein. We measured brush-border uptakes of seven AAs that variously serve as substrates for four AA transporters, and brush-border and cytosolic activities of four peptidases. The three rations yielded essentially the same AA uptake rates. Peptidase activities tended to be lower on the AA ration than on the protein ration. In other studies, all three rations yielded the same rates of brush-border peptide uptake; protein is only modestly more effective than AAs at inducing synthesis of pancreatic proteases; and, depending on the animal species, protein is either much less or much more effective than AAs at stimulating release of cholecystokinin and hence of pancreatic enzymes. Thus the regulators of each process involved in protein digestion are not necessarily that process's substrate. We call attention to other cases in which the functional significance of regulatory signals remains to be understood.

scholarly journals Synthetic and Crystalline Amino Acids: Alternatives to Soybean Meal in Chicken-Meat Production

Animals ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 729 ◽  
Author(s):  
Peter H. Selle ◽  
Juliano Cesar de Paula Dorigam ◽  
Andreas Lemme ◽  
Peter V. Chrystal ◽  
Sonia Y. Liu
Keyword(s):  
Amino Acids ◽  
Soybean Meal ◽  
Broiler Chickens ◽  
Crude Protein ◽  
Chicken Meat ◽  
Meat Production ◽  
Dietary Crude Protein ◽  
Reduced Crude Protein ◽  
Crystalline Amino Acids ◽  
Protein Diets

: This review explores the premise that non-bound (synthetic and crystalline) amino acids are alternatives to soybean meal, the dominant source of protein, in diets for broiler chickens. Non-bound essential and non-essential amino acids can partially replace soybean meal so that requirements are still met but dietary crude protein levels are reduced. This review considers the production of non-bound amino acids, soybeans, and soybean meal and discusses the concept of reduced-crude protein diets. There is a focus on specific amino acids, including glycine, serine, threonine, and branched-chain amino acids, because they may be pivotal to the successful development of reduced-crude protein diets. Presently, moderate dietary crude protein reductions of approximately 30 g/kg are feasible, but more radical reductions compromise broiler performance. In theory, an ‘ideal’ amino acid profile would prevent this, but this is not necessarily the case in practice. The dependence of the chicken-meat industry on soybean meal will be halved if crude protein reductions in the order of 50 g/kg are attained without compromising the growth performance of broiler chickens. In this event, synthetic and crystalline, or non-bound, amino acids will become viable alternatives to soybean meal in chicken-meat production.

Epigenetic Mechanisms of Maternal Dietary Protein and Amino Acids Affecting Growth and Development of Offspring

2019 ◽  
Vol 20 (7) ◽  
pp. 727-735 ◽  
Author(s):  
Yi Wu ◽  
Zhibin Cheng ◽  
Yueyu Bai ◽  
Xi Ma
Keyword(s):  
Amino Acids ◽  
Dna Methylation ◽  
Dietary Protein ◽  
Growth And Development ◽  
Later Life ◽  
Biological Macromolecules ◽  
Epigenetic Mechanisms ◽  
Maternal Circulation ◽  
Energy Processing ◽  
Living Organisms

Nutrients can regulate metabolic activities of living organisms through epigenetic mechanisms, including DNA methylation, histone modification, and RNA regulation. Since the nutrients required for early embryos and postpartum lactation are derived in whole or in part from maternal and lactating nutrition, the maternal nutritional level affects the growth and development of fetus and creates a profound relationship between disease development and early environmental exposure in the offspring’s later life. Protein is one of the most important biological macromolecules, involved in almost every process of life, such as information transmission, energy processing and material metabolism. Maternal protein intake levels may affect the integrity of the fetal genome and alter DNA methylation and gene expression. Most amino acids are supplied to the fetus from the maternal circulation through active transport of placenta. Some amino acids, such as methionine, as dietary methyl donor, play an important role in DNA methylation and body’s one-carbon metabolism. The purpose of this review is to describe effects of maternal dietary protein and amino acid intake on fetal and neonatal growth and development through epigenetic mechanisms, with examples in humans and animals.

scholarly journals The Role of Reduced Methionine in Mediating the Metabolic Responses to Protein Restriction Using Different Sources of Protein

Nutrients ◽  
2021 ◽  
Vol 13 (8) ◽  
pp. 2609
Author(s):  
Han Fang ◽  
Kirsten P. Stone ◽  
Sujoy Ghosh ◽  
Laura A. Forney ◽  
Thomas W. Gettys
Keyword(s):  
Amino Acids ◽  
Dietary Protein ◽  
Target Genes ◽  
Protein Restriction ◽  
Metabolic Phenotype ◽  
Sulfur Amino Acids ◽  
Transcriptional Responses ◽  
Similar Reduction ◽  
Dietary Protein Restriction ◽  
Methionine Restriction

Dietary protein restriction and dietary methionine restriction (MR) produce a comparable series of behavioral, physiological, biochemical, and transcriptional responses. Both dietary regimens produce a similar reduction in intake of sulfur amino acids (e.g., methionine and cystine), and both diets increase expression and release of hepatic FGF21. Given that FGF21 is an essential mediator of the metabolic phenotype produced by both diets, an important unresolved question is whether dietary protein restriction represents de facto methionine restriction. Using diets formulated from either casein or soy protein with matched reductions in sulfur amino acids, we compared the ability of the respective diets to recapitulate the metabolic phenotype produced by methionine restriction using elemental diets. Although the soy-based control diets supported faster growth compared to casein-based control diets, casein-based protein restriction and soy-based protein restriction produced comparable reductions in body weight and fat deposition, and similar increases in energy intake, energy expenditure, and water intake. In addition, the prototypical effects of dietary MR on hepatic and adipose tissue target genes were similarly regulated by casein- and soy-based protein restriction. The present findings support the feasibility of using restricted intake of diets from various protein sources to produce therapeutically effective implementation of dietary methionine restriction.

DIGESTION OF NUTRIENTS IN THE SMALL INTESTINE OF PIGS FED DIETS CONTAINING RAW AND AUTOCLAVED FABA BEANS

1976 ◽  
Vol 56 (3) ◽  
pp. 451-456 ◽  
Author(s):  
M. IVAN ◽  
J. P. BOWLAND
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Beneficial Effect ◽  
Dietary Protein ◽  
Dry Matter ◽  
Latin Square ◽  
Sole Source ◽  
Intestinal Uptake ◽  
Gross Energy ◽  
Faba Beans

Four castrated pigs, each fitted with a re-entrant cannula in the terminal ileum, were used to study digestion in the small intestine. A nitrogen-free diet was used for the estimation of metabolic nitrogen and amino acids. Faba beans, as the sole source of dietary protein, were used raw or after autoclaving for 30 or 60 min. The four diets were fed to the pigs in a 4 × 4 latin square experiment. The pigs were fed each diet for 6 days prior to a 24-hr collection of total ileal contents. Autoclaving of faba beans had no significant effect on digestibility of dry matter, gross energy, nitrogen and individual amino acids except arginine, which was significantly increased. The intestinal uptake of arginine was the highest and of cystine the lowest in all faba bean diets. It was concluded that autoclaving faba beans had no beneficial effect on the digestion of nutrients in the small intestine of the pig.

scholarly journals Repletion of branched chain amino acids reverses mTORC1 signaling but not improved metabolism during dietary protein dilution

2017 ◽  
Vol 6 (8) ◽  
pp. 873-881 ◽  
Author(s):  
Adriano Maida ◽  
Jessica S.K. Chan ◽  
Kim A. Sjøberg ◽  
Annika Zota ◽  
Dieter Schmoll ◽  
...  
Keyword(s):  
Amino Acids ◽  
Dietary Protein ◽  
Branched Chain Amino Acids ◽  
Mtorc1 Signaling ◽  
Branched Chain

Dietary protein paradox: decrease of amino acid availability induced by high-protein diets

1993 ◽  
Vol 264 (6) ◽  
pp. G1057-G1065 ◽  
Author(s):  
C. Moundras ◽  
C. Remesy ◽  
C. Demigne
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Dietary Protein ◽  
High Protein ◽  
Glutamine Metabolism ◽  
Metabolic Adaptation ◽  
Casein Diet ◽  
Serine Dehydratase ◽  
High Protein Diets ◽  
Protein Diets

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)

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