scholarly journals Nonessential amino acid usage for protein replenishment in humans: a method of estimation

2019 ◽  
Vol 110 (2) ◽  
pp. 255-264 ◽  
Author(s):  
Paolo Tessari
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Quality ◽  
Essential Amino Acids ◽  
World Health ◽  
Whole Body ◽  
Published Data ◽  
Total Proteins ◽  
Body Protein ◽  
Amino Acid Turnover

ABSTRACT Background Essential amino acids (EAAs) are key factors in determining dietary protein quality. Their RDAs have been estimated. However, although nonessential amino acids (NEAAs) are utilized for protein synthesis too, no estimates of their usage for body protein replenishment have been proposed so far. Objective The aim of this study was to provide minimum, approximate estimates of NEAA usage for body protein replenishment/conservation in humans. Methods A correlation between the pattern of both EAAs and NEAAs in body proteins, and their usage, was assumed. In order to reconstruct an “average” amino acid pattern/composition of total body proteins (as grams of amino acid per gram of protein), published data of relevant human organs/tissues (skeletal muscle, liver, kidney, gut, and collagen, making up ∼74% of total proteins) were retrieved. The (unknown) amino acid composition of residual proteins (∼26% of total proteins) was assumed to be the same as for the sum of the aforementioned organs excluding collagen. Using international EAA RDA values, an average ratio of EAA RDA to the calculated whole-body EAA composition was derived. This ratio was then used to back-calculate NEAA usage for protein replenishment. The data were calculated also using estimated organ/tissue amino acid turnover. Results The individual ratios of World Health Organization/Food and Agriculture Organization/United Nations University RDA to EAA content ranged between 1.35 (phenylalanine + tyrosine) and 3.68 (leucine), with a mean ± SD value of 2.72 ± 0.81. In a reference 70-kg subject, calculated NEAA usage for body protein replenishment ranged from 0.73 g/d for asparagine to 3.61 g/d for proline. Use of amino acid turnover data yielded similar results. Total NEAA usage for body protein replenishment was ∼19 g/d (45% of total NEAA intake), whereas ∼24 g/d was used for other routes. Conclusion This method may provide indirect minimum estimates of the usage of NEAAs for body protein replacement in humans.

scholarly journals Consumption of a Specially-Formulated Mixture of Essential Amino Acids Promotes Gain in Whole-Body Protein to a Greater Extent than a Complete Meal Replacement in Older Women with Heart Failure

Nutrients ◽  
2019 ◽  
Vol 11 (6) ◽  
pp. 1360 ◽  
Author(s):  
Il-Young Kim ◽  
Sanghee Park ◽  
Ellen T. H. C. Smeets ◽  
Scott Schutzler ◽  
Gohar Azhar ◽  
...  
Keyword(s):  
Heart Failure ◽  
Amino Acids ◽  
Amino Acid ◽  
Body Mass ◽  
Essential Amino Acids ◽  
Whole Body ◽  
Meal Replacement ◽  
Anabolic Response ◽  
Body Protein ◽  
Net Protein

Heart failure in older individuals is normally associated with a high body mass index and relatively low lean body mass due to, in part, a resistance to the normal anabolic effect of dietary protein. In this study we have investigated the hypothesis that consumption of a specially-formulated composition of essential amino acids (HiEAAs) can overcome anabolic resistance in individuals with heart failure and stimulate the net gain of body protein to a greater extent than a commercially popular protein-based meal replacement beverage with greater caloric but lower essential amino acid (EAA) content (LoEAA). A randomized cross-over design was used. Protein kinetics were determined using primed continuous infusions of L-(2H5)phenylalanine and L-(2H2)tyrosine in the basal state and for four hours following consumption of either beverage. Both beverages induced positive net protein balance (i.e., anabolic response). However, the anabolic response was more than two times greater with the HiEAA than the LoEAA (p < 0.001), largely through a greater suppression of protein breakdown (p < 0.001). Net protein accretion (g) was also greater in the HiEAA when data were normalized for either amino acid or caloric content (p < 0.001). We conclude that a properly formulated EAA mixture can elicit a greater anabolic response in individuals with heart failure than a protein-based meal replacement. Since heart failure is often associated with obesity, the minimal caloric value of the HiEAA formulation is advantageous.

Meal stimulation of albumin synthesis: a significant contributor to whole body protein synthesis in humans

1992 ◽  
Vol 263 (4) ◽  
pp. E794-E799 ◽  
Author(s):  
P. De Feo ◽  
F. F. Horber ◽  
M. W. Haymond
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Combined Treatment ◽  
Essential Amino Acids ◽  
Whole Body ◽  
Albumin Synthesis ◽  
Body Protein ◽  
Peripheral Tissues ◽  
Stimulation Of

The present studies were performed to test the hypothesis that the liver, by increasing the synthesis of specific plasma proteins during the absorption of an amino acid meal, may play an important role in the temporary "storage" of ingested essential amino acids and to explore the effects of glucocorticosteroids and recombinant human growth hormone (rhGH) on these processes. The fractional synthetic rates of albumin and fibrinogen were determined using simultaneous infusions of intravenous [1-14C]leucine and intraduodenal [4,5-3H]leucine after 22 h fasting and during absorption of glucose and amino acids in four groups of normal subjects treated for 1 wk with placebo, prednisone (0.8 mg.kg-1.day-1), rhGH (0.1 mg.kg-1.day-1), or combined treatment. When compared with the fasted state and independent of the route of tracer delivery and hormonal treatment, albumin, but not fibrinogen, synthesis increased (P < 0.0001) during absorption of a mixed glucose amino acid meal in all groups. This increase in albumin synthesis accounted for 28% of the increase in whole body protein synthesis associated with feeding and for 24, 22, and 14% in the prednisone, rhGH, and combined treatment groups, respectively. These data suggest that the stimulation of albumin synthesis observed during feeding prevents irreversible oxidative losses of a significant fraction of ingested essential amino acids and may serve as a vehicle to capture excess dietary amino acids and transport them to peripheral tissues to sustain local protein synthesis.

scholarly journals Splanchnic-bed transfers of amino acids in sheep blood and plasma, as monitored through use of a multiple U-13C-labelled amino acid mixture

1996 ◽  
Vol 75 (2) ◽  
pp. 217-235 ◽  
Author(s):  
G. E. Lobley ◽  
A. Connell ◽  
D. K. Revell ◽  
B. J. Bequette ◽  
D. S. Brown ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Essential Amino Acids ◽  
Whole Body ◽  
Gas Chromatography Mass Spectrometry ◽  
Acid Mixture ◽  
Body Protein ◽  
Hydrolysis Of

AbstractThe response in whole-body and splanchnic tissue mass and isotope amino acid transfers in both plasma and blood has been studied in sheep offered 800 g lucerne (Medicago sutiva) pellets/d. Amino acid mass transfers were quantified over a 4 h period,by arterio-venous procedures, across the portal-drained viscera (PDV) and liver on day 5 of an intravenous infusion of either vehicle or the methylated products, choline (0.5 g/d) plus creatine (10 g/d). Isotopic movements were monitored over the same period during a 10 h infusion of a mixture of U-13C-labelled amino acids obtained from hydrolysis of labelled algal cells. Sixteen amino acids were monitored by gas chromatography-mass spectrometry, with thirteen of these analysed within a single chromatographic analysis. Except for methionine, which is discussed in a previous paper, no significant effects of choline plus creatine infusion were observed on any of the variables reported. Whole-body protein irreversible-loss rates ranged from 158 to 245 g/d for the essential amino acids, based on the relative enrichments (dilution of the U-13C molecules by those unlabelled) of free amino acids in arterial plasma, and 206-519 g/d, when blood free amino acid relative enrichments were used for the calculations. Closer agreement was obtained between lysine, threonine, phenylalanine and the branched-chain amino acids. Plasma relative enrichments always exceeded those in blood (P < 0.001), possibly due to hydrolysis of peptides or degradation of protein within the erythrocyte or slow equilibration between plasma and the erythrocyte. Net absorbed amino acids across the PDV were carried predominantly in the plasma. Little evidence was obtained of any major and general involvement of the erythrocytes in the transport of free amino acids from the liver. Net isotope movements also supported these findings. Estimates of protein synthesis rates across the PDV tissues from [U-13C] leucine kinetics showed good agreement with previous values obtained with single-labelled leucine. Variable rates were obtained between the essential amino acids, probably due to different intracellular dilutions. Isotope dilution across the liver was small and could be attributed predominantly to uni-directional transfer from extracellular sources into the hepatocytes and this probably dominates the turnover of the intracellular hepatic amino acid pools.

Nutritionally non-essential amino acids are dispensable for whole-body protein synthesis after exercise in endurance athletes with an adequate essential amino acid intake

Amino Acids ◽  
2018 ◽  
Vol 50 (12) ◽  
pp. 1679-1684 ◽  
Author(s):  
Hiroyuki Kato ◽  
Kimberly A. Volterman ◽  
Daniel W. D. West ◽  
Katsuya Suzuki ◽  
Daniel R. Moore
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Essential Amino Acid ◽  
Essential Amino Acids ◽  
Endurance Athletes ◽  
Whole Body ◽  
Body Protein ◽  
Acid Intake ◽  
Amino Acid Intake

scholarly journals EFFECT OF STORAGE TIME ON THE QUALITY OF SMOKED HETEROCLARIAS

2020 ◽  
Vol 25 (2) ◽  
pp. 30
Author(s):  
Ayodeji Ahmed Ayeloja ◽  
W. A. Jimoh ◽  
T. O. Uthman ◽  
M. O. Shittu
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Storage Time ◽  
Protein Quality ◽  
Storage Period ◽  
Essential Amino Acids ◽  
Vulnerable Groups ◽  
Average Weight ◽  
Duration Of Storage

Effect of storage time on the quality of smoked heteroclarias was studied. 108 samples of heteroclarias (average weight 210 + 15g) was used. Analysis carried out include: proximate, mineral composition (Ca, Na, Fe and Mg), biochemical, amino acid and sensory evaluation. Data obtained was subjected to Analysis of Variance (ANOVA) while the sensory data was subjected to nonparametric test (Kruskal Wallis test). Smoked heteroclarias have good nutritional quality in terms of proximate, mineral and amino acids all of which decrease with increase in duration of storage at ambient temperatures. Glutamic acid  was the most predominant amino acid and the highest non-essential amino acid (NEEA), lysine was the most predominant EAA. There was higher concentration of non-essential amino acids than essential amino acids, EAA/NEAA ratio (0.86 – 0.93) recorded indicates that the fish have excellent protein quality; its the predicted protein efficiency ratio (P-PER) ranged between 3.44-3.61 and its biological value ranged between 79.84 -75.04. Its chemical score and TEAA decrease with increase in storage time. Its texture quality reduced significantly (χ2 = 12.207, p<0.01) with increased storage period. It is therefore recommended that smoked heteroclarias be consumed as soon as it is smoked and regularly for good healthy conditions especially among children, aged and other vulnerable groups.

Amino acids suppress proteolysis independent of insulin throughout the neonatal period

1997 ◽  
Vol 272 (4) ◽  
pp. E592-E599 ◽  
Author(s):  
B. B. Poindexter ◽  
C. A. Karn ◽  
J. A. Ahlrichs ◽  
J. Wang ◽  
C. A. Leitch ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Neonatal Period ◽  
Essential Amino Acids ◽  
Whole Body ◽  
Amino Acid Availability ◽  
Dose Dependent Fashion ◽  
Term Newborns ◽  
Dose Dependent ◽  
Acid Administration

To determine how increased amino acid availability alters rates of whole body proteolysis and the irreversible catabolism of the essential amino acids leucine and phenylalanine throughout the neonatal period, leucine and phenylalanine kinetics were measured under basal conditions and in response to intravenous amino acids in two separate groups of healthy, full-term newborns (at 3 days and 3 wk of age). The endogenous rates of appearance of leucine and phenylalanine (reflecting proteolysis) were suppressed equally in both groups and in a dose-dependent fashion (by approximately 10% with 1.2 g x kg(-1) x day(-1) and by approximately 20% with 2.4 g x kg(-1) x day(-1)) in response to intravenous amino acid delivery. Insulin concentrations remained unchanged from basal values during amino acid administration. The irreversible catabolism of leucine and phenylalanine increased in a stepwise fashion in response to intravenous amino acids; again, no differences were observed between the two groups. This study clearly demonstrates that the capacity to acutely increase rates of leucine oxidation and phenylalanine hydroxylation is fully present early in the neonatal period in normal newborns. Furthermore, these data suggest that amino acid availability is a primary regulator of proteolysis in normal newborns throughout the neonatal period.

scholarly journals COMPARISON OF AMINO ACIDS IN 8 DIFFERENT BOILED TROPICAL FRUITS

2019 ◽  
pp. 21-23
Author(s):  
Radha Palaniswamy ◽  
Dhanyasri Selvaraj ◽  
Sandhiya Renganathan
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Content ◽  
Protein Quality ◽  
Amino Acid Content ◽  
Essential Amino Acids ◽  
Tropical Fruits ◽  
Good Balance

Objective: To determine the protein quality, especially the amino acid content of 8 tropical fruits both raw and boiled samples. Eight different tropical fruits were used in the study (Apricot, Jamun, Dragonfruit, Pomegranate, Mangustan, Litchi, Jackfruit, and Kiwi.Methods: Ninhydrin method was used for the estimation of the concentration of amino acids present in the above fruits. Raw and boiled fruits were used for the study.Results: Both raw and boiled forms which showed thats Jamun and Mangustan contained highest concentration amino acids whereas apricot shows the lowest concentration of amino acids except in Jamun which showed higher values in the raw fruit whereas in others the boiled samples showed higher values.Conclusion: It was evident that tropical fruits have a good balance of the essential amino acids (both raw and boiled fomr) which provide significant sources of protein in our diet.

Comparison of Interlaboratory Variation in Amino Acid Analysis and Rat Growth Assays for Evaluating Protein Quality

1985 ◽  
Vol 68 (1) ◽  
pp. 52-56 ◽  
Author(s):  
Ghulam Sarwar ◽  
Robert Blair ◽  
Mendel Friedman ◽  
Michael R Gumbmann ◽  
Ross L Hackler ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Protein Quality ◽  
Essential Amino Acids ◽  
Quality Indices ◽  
Protein Ratio ◽  
Protein Sources ◽  
Rat Growth ◽  
Positive Correlations

Abstract Estimates of inter- and intralaboratory variation of protein efficiency ratio (PER), relative PER (RPER), net protein ratio (NPR), relative NPR (RNPR), and nitrogen utilization (NU) were compared with those of amino acid analysis in the same batches of 7 protein sources (ANRC casein, egg white solids, minced beef, soy assay protein, rapeseed protein concentrate, pea flour, and whole wheat flour). Interlaboratory variation (estimated as between-laboratories coefficients of variation, CV) of NPR and RNPR (up to 6.0%) was lower than that of PER (up to 20.2%) and RPER (up to 18.5%). The interlaboratory determination of NPR and RNPR was also more reproducible than that of most essential amino acids (CV up to 10.0%), especially tryptophan (CV up to 23.7%), cystine (CV up to 17.6%), and methionine (CV up to 16.1%). Intralaboratory variation (estimated as within-laboratories CV) of amino acid analysis (up to 4.7%), however, was comparable to that of protein quality indices in most protein sources (up to 6.0%). The significant (P &lt;0.01) positive correlations (r = 0.68-0.74) between amino acid scores and protein quality indices based on rat growth were further improved when amino acid scores were corrected for digestibility of protein (r = 0.73-0.78) or individual amino acids (r = 0.79- 0.82).

scholarly journals Advantages and limitations of the protein digestibility-corrected amino acid score (PDCAAS) as a method for evaluating protein quality in human diets

2012 ◽  
Vol 108 (S2) ◽  
pp. S333-S336 ◽  
Author(s):  
Gertjan Schaafsma
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Quality ◽  
Protein Digestibility ◽  
Essential Amino Acids ◽  
Tissue Growth ◽  
Biological Efficiency ◽  
Amino Acid Supplementation ◽  
Reference Pattern ◽  
Plant Protein Sources

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.

Protein degradation and synthesis measured with multiple amino acid tracers in vivo

1996 ◽  
Vol 271 (4) ◽  
pp. E733-E741 ◽  
Author(s):  
P. Tessari ◽  
R. Barazzoni ◽  
M. Zanetti ◽  
M. Vettore ◽  
S. Normand ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein S ◽  
Essential Amino Acids ◽  
Body Protein ◽  
Amino Acid Availability ◽  
Before And After ◽  
Branched Chain ◽  
Multiple Amino Acid

Whether tracers of different essential amino acids yield the same estimates of body protein turnover is still uncertain. Therefore, we have simultaneously determined leucine (Leu; using [14C]Leu), phenylalanine (Phe; using [13C]Phe), and tyrosine (Tyr; using [2H2]Tyr) rates of appearance (Ra) from proteolysis (PD), as well as Leu and Phe disposal, into protein synthesis (PS) both before and after an anabolic stimulus in healthy volunteers. Protein anabolism was stimulated by insulin plus a branched-chain amino acid-enriched aromatic amino acid-deficient amino acid solution, which increased Leu (from 145 +/- 9 to 266 +/- 10 mumol/l) but decreased Phe (from 57 +/- 2 to 46 +/- 3) and Tyr (from 58.7 +/- 5.5 to 21.0 +/- 2.2) concentrations. Postabsorptive endogenous Leu Ra (2.04 +/- 0.12 mumol.kg-1.min-1), Phe Ra (0.66 +/- 0.03), and Tyr Ra (0.45 +/- 0.06), as well as rates of PS determined with the leucine (1.65 +/- 0.10 mumol.kg-1.min-1) and the phenylalanine tracer (0.57 +/- 0.03), agreed well with the known abundance of these amino acids in body protein(s). After insulin and amino acids, PD was suppressed (P < 0.001) using all tracers. However, although percent suppression of endogenous Leu Ra (-->1.49 +/- 0.10 mumol.kg-1.min-1, 26 +/- 5%) and Phe Ra (-->0.53 +/- 0.02 mumol.kg-1.min-1, -20 +/- 2%) were comparable, endogenous Tyr Ra was suppressed to a larger extent (-->0.23 +/- 0.02 mumol.kg-1.min-1, -46 +/- 3% P = 0.038). PS was stimulated using the Leu (+24 +/- 7%, P < 0.02) but not the Phe (+6 +/- 4%, not significant) data. We conclude that isotopes of different essential amino acid: provide comparable estimates of PD and PS in the postabsorptive state. However, their responses to an anabolic stimulus may differ, possibly depending on exogenous amino acid availability and/or the resulting plasma levels.

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