Dipeptide utilization by starter streptococci

1977 ◽  
Vol 44 (2) ◽  
pp. 309-317 ◽  
Author(s):  
B. A. Law
Keyword(s):  
Amino Acids ◽  
Transport System ◽  
Free Amino Acids ◽  
Free Amino ◽  
Essential Amino Acids ◽  
Exponential Phase ◽  
Whole Cells ◽  
Streptococcus Cremoris ◽  
Defined Media ◽  
Hydrolysis Of

SummaryOf 8 strains ofStreptococcus cremoristested, 5 grew almost as well in defined media in which various essential amino acids were supplied in dipeptides as they did in media containing the equivalent free amino acids. The remainder grew poorly or not at all in the peptide-containing media. Growth of peptide-utilizing strains was inhibited by also including structurally-related dipeptides in the medium, presumably due to competition for uptake by transport system carriers. Both types of starters produced cell-free dipeptidases recoverable from the medium of exponential phase cultures. Addition of the partly-purified extracellular dipeptidases to dipeptidecontaining test media initiated growth in strains unable to use peptides.Str. lactisgrew in defined peptide media, but the further addition of structurally-related dipeptides did not inhibit growth, either bcause each dipeptide was transported by a specific carrier or because peptides were hydrolysed extracellularly. The presence of cell-bound extracellular dipeptidase was indicated by the hydrolysis of dipeptides with washed whole cells in buffer. This was not observed withStr. cremorisstrains.

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.

scholarly journals FREE AMINO ACIDS AND NUCLEIC ACID CONTENT OF CELL NUCLEI ISOLATED BY A MODIFICATION OF BEHRENS' TECHNIQUE

1950 ◽  
Vol 33 (5) ◽  
pp. 629-642 ◽  
Author(s):  
Alexander L. Dounce ◽  
Garson H. Tishkoff ◽  
Shirley R. Barnett ◽  
Richard M. Freer
Keyword(s):  
Amino Acids ◽  
Nucleic Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Essential Amino Acids ◽  
Nucleic Acid Content ◽  
Cell Nuclei ◽  
Whole Cells ◽  
Cell Fractions ◽  
Isolated Cell

1. Nuclei were prepared from frozen rat liver by a modification of the technique of Behrens, and were studied with regard to the content of free amino acids and nucleic acid. 2. Under rigorously controlled conditions, preparations of nuclei are obtained by the Behrens' method which form a gel in the presence of 5 or 10 per cent NaCl or of water plus a small amount of dilute alkali; whereas when conditions are less rigorously controlled, nuclei are obtained which form no such gel. The property of forming gels with alkali is probably characteristic of all cell nuclei which have not undergone autolysis. 3. Nuclei prepared by the Behrens' technique contain the enzymes arginase, catalase, and esterase in very appreciable concentrations. 4. The free amino acids of the isolated cell nuclei, as well as of other liver cell fractions, have been investigated using the technique of paper chromatography. 5. The chromatographic patterns of the free amino acids of whole cells, ground cytoplasm, and isolated cell nuclei were very similar or identical. A feature of interest in these chromatograms was the faintness or absence of the spots due to a number of the essential amino acids, as compared to the intensities of the spots due to glycine, alanine, and glutamic acid. Glutathione was present in the isolated nuclei as well as in the whole cells. 6. Chromatograms made from hydrolysates of nuclei showed high concentrations of the essential amino acids and were similar to chromatograms of hydrolysates of typical proteins.

Availability of amino acids supplied by constant intravenous infusion of synthetic dipeptides in healthy man

1989 ◽  
Vol 76 (6) ◽  
pp. 643-648 ◽  
Author(s):  
S. Albers ◽  
J. Wernerman ◽  
P. Stehle ◽  
E. Vinnars ◽  
P. Fürst
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Metabolic Clearance ◽  
Amino Acid Solution ◽  
Appreciable Change ◽  
Total Body ◽  
Hydrolysis Of ◽  
Firm Evidence ◽  
Apparently Healthy

1. A commercial amino acid solution supplemented with two synthetic dipeptides, l-alanyl-l-glutamine (Ala-Gln) and glycyl-l-tyrosine (Gly-Tyr), or alternatively with isonitrogenous amounts of free alanine and glycine has been continuously infused over 4 h in six apparently healthy volunteers. 2. The infusion of the solutions was not accompanied by any side effects and the volunteers reported no complaints. 3. Infusion of the alanine- and glycine-supplemented control solution resulted in an increase of the concentration of these amino acids, while no appreciable change in free glutamine concentration was observed and free tyrosine revealed a steady decrease throughout the infusion. 4. Infusion of the peptide-supplemented solution resulted in a prompt equimolar liberation of the constituent free amino acids (glutamine, alanine, tyrosine and glycine), approaching steady state after about 30 min infusion, while only trace but stable concentrations of the two dipeptides were measured throughout the infusion. No peptides were detectable in urine. The findings suggest a nearly quantitative extracellular hydrolysis of the infused dipeptides and indicate a subsequent utilization of the liberated free amino acids. 5. The estimated metabolic clearance rates and total body plasma clearances were very similar for the two dipeptides (Ala-Gln 35.9 ± 9.5 ml min−1 kg−1 and 2.9 ± 0.9 1/min, respectively; Gly-Tyr 33.7 ± 9.5 ml min−1 kg−1 and 2.7 ± 0.9 1/min, respectively); thus there is little difference in the metabolic handling of these dipeptides. 6. The study provides firm evidence that the synthetic dipeptides Ala-Gln and Gly-Tyr are quantitatively hydrolysed and that these peptides can be used as a safe and efficient source of free glutamine and tyrosine as part of a commercial solution.

Free Amino Acids in Citrullus vulgaris (Watermelon)

PEDIATRICS ◽  
1984 ◽  
Vol 73 (6) ◽  
pp. 879-879
Author(s):  
T. A. TEDESCO ◽  
S. A. BENFORD ◽  
R. C. FOSTER ◽  
L. A. BARNESS
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Neonatal Period ◽  
Essential Amino Acids ◽  
Solid Foods ◽  
Citrullus Vulgaris ◽  
Keto Acids ◽  
Wet Weight ◽  
Cycle Disorders

To the Editor.— Currently accepted dietary management of citrullinemia and other urea cycle disorders includes protein restriction, sodium benzoate, and dietary supplements of keto acids or essential amino acids with postblock intermediates such as arginine in citrullinemia and arginino-succinic aciduria. When a child survives the neonatal period on such a regimen and solid foods are introduced into the diet, there is at least one fruit that should be avoided, Citrullus Vulgaris, commonly known as watermelon. Quantitation of free amino acids extracted from 1 g wet weight of watermelon fruit yielded the following (in mmoles per gram wet weight): Phenylalanine, 1.25; histidine, 0.24; tryptophan, 0.35; lysine, 0.82; ornithine, 0.32; arginine, 11.36; aspartic acid, 0.97; threonine, 0.74; serine, 1.05; glutamine, 3.86; glutamic acid, 1.38; citrulline, 23.68; alanine, 1.15; valine, 0.17; isoleucine, 1.24; leucine, 0.24.

scholarly journals Isolation of Free Amino Acids via Enzymatic Hydrolysis of Tobacco-Derived F1 Protein

2018 ◽  
Vol 28 (4) ◽  
pp. 179-190
Author(s):  
Mehdi Ashraf-Khorassani ◽  
William M. Coleman ◽  
Michael F. Dube ◽  
Larry T. Taylor
Keyword(s):  
Amino Acids ◽  
Enzymatic Hydrolysis ◽  
Free Amino Acids ◽  
Free Amino ◽  
Protein Concentration ◽  
Enzyme Concentration ◽  
Enzymatic Conversion ◽  
Reaction Conditions ◽  
Analytical Methodology ◽  
Hydrolysis Of

SummaryFree amino acids have been isolated via optimized enzymatic hydrolysis of F1 tobacco protein using two cationic resins (Amberlite IR120 and Dowex MAC-2). Optimized enzymatic conversions of the protein as a result of systematic variations in conditions (e.g., time, temperature, pH, enzyme type, enzyme concentration, anaerobic/aerobic environments, and protein concentration) employing commercially available enzymes, were consistently higher than 50% with qualitative amino acid arrays that were consistent with the known composition of tobacco F1 protein. Amberlite IR120 was shown to have a much higher efficiency and capacity for isolation of amino acids from standard solutions and from hydrolysate when compared with the results using Dowex MAC-2. Two columns packed with conditioned Amberlite IR120 (120 × 10 mm,12–15 g resin) and (200 × 25.4 mm, 60–65 g resin) were used to isolate two batches (2.5–3.0 mg and 13–15 mg) of free amino acids, respectively. A relatively inexpensive analytical methodology was developed for rapid analysis of the free amino acids contained within the enzyme hydrolysate. Commercially available enzymes, when employed in optimized reaction conditions, are very effective for enzymatic conversion of tobacco F1 protein to free amino acids.

The effect of starvation and low nitrogen intakes on the concentration of free amino acids in the blood plasma and on the nitrogen metabolism in sheep

1970 ◽  
Vol 21 (5) ◽  
pp. 723 ◽  
Author(s):  
J Leibholz
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Dry Matter ◽  
Control Diet ◽  
Amino Nitrogen ◽  
Essential Amino Acids ◽  
Isoleucine Leucine ◽  
Plasma Urea ◽  
Low Nitrogen

Crossbred wethers were given a control diet (8 g nitrogen, 730 g dry matter daily) or a low nitrogen diet (0.5 g nitrogen, 520 g dry matter daily) or starved, for a 12 or 20 day experimental period. The concentrations of free serine, glutamine, glycine, alanine, histidine, and arginine in the plasma of the starved sheep decreased significantly while the concentrations of lysine, 3-methylhistidine, and isoleucine increased significantly. The ratio of essential to non-essential amino acids increased from 0.35 to 0.56 in the starved sheep. In sheep on the low nitrogen diet, the ratio of essential to non-essential amino acids in the plasma decreased from 0.40 to 0.27, with significant increases in the concentrations of glutanlic acid, glutamine, glycine, isoleucine, leucine, and 3-methylhistidine. Starvation and the low nitrogen diet both resulted in a reduction of the plasma urea concentrations. Starvation and the low nitrogen diet resulted in a 20-50 % reduction in the flow of saliva and a 40-78% increase in the concentration of total nitrogen. This resulted in no significant change in the daily secretion of nitrogen in the saliva. The concentration of urea in the saliva was increased by 3-54%. The concentrations of individual free amino acids in saliva are reported. The nitrogen content of the rumen was reduced, and after 7 days of starvation or on the low nitrogen diet all rumen nitrogen could be attributed to ammonia and free �-amino nitrogen.

Effect of Aging on Free Amino Acids and Electrolytes in Leg Skeletal Muscle

1979 ◽  
Vol 56 (5) ◽  
pp. 427-432 ◽  
Author(s):  
P. Möller ◽  
J. Bergström ◽  
S. Eriksson ◽  
P. Fürst ◽  
K. Hellström
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Statistical Significance ◽  
Plasma Concentrations ◽  
The Elderly ◽  
Essential Amino Acids ◽  
Elderly Men ◽  
Healthy Elderly ◽  
The Difference

1. The concentrations of electrolytes and free amino acids in plasma and the quadriceps femoris muscle were studied in ten apparently healthy elderly men, 52–77 years of age. The results were compared with those previously recorded for men 20–36 years old. 2. The two groups of subjects did not differ with regard to serum electrolytes and intracellular water content but the extracellular water in the older subjects exceeded that of the younger group by about 50%. The muscle specimens of the elderly men were also characterized by a 40% elevation of their total contents of Na+ and Cl−, whereas the content of K+ and Mg2+ was almost identical in both groups. 3. The means recorded for the plasma concentrations of most amino acids tended to be higher in the elderly men. The differences reached statistical significance for tyrosine, histidine, valine, lysine and total essential amino acids. In keeping with the findings in plasma, the amino acid concentrations in the muscle of the older group tended to exceed those of the younger ones. The difference reached statistical significance with regard to total amino acids, essential and non-essential amino acids, aspartate, alanine, citrulline, histidine, arginine, leucine and lysine. The various mechanisms that may contribute to these findings are discussed.

Utilization of amino acids by pre-ruminant lambs. III.* The influence of age and the dietary proportions of essential and non-essential amino acids on the levels of urea, ammonia and free amino acids in the blood plasma of milk-fed lambs

1978 ◽  
Vol 29 (1) ◽  
pp. 145 ◽  
Author(s):  
H Dove
Keyword(s):  
Amino Acids ◽  
Plasma Levels ◽  
Free Amino Acids ◽  
Free Amino ◽  
Essential Amino Acids ◽  
High Plasma ◽  
Whole Milk ◽  
Wide Range ◽  
Pattern Characteristic ◽  
Pre Treatment

Jugular blood samples were obtained from 10.5 kg and 28 kg lambs receiving a diet of reconstituted cows' whole milk. The lambs were then given diets in which the proportion of essential amino acids (BAA) in the dietary crude protein was altered over a wide range. A second blood sample was taken after lambs had received such diets for 12 days. Plasma obtained from these samples was analysed for free amino acids, urea and ammonia. The pattern of plasma free amino acids (PFAA) in lambs given reconstituted cows' whole milk is described. In both the pre-treatment and post-treatment samples, the heavier lambs appeared to have lower plasma levels of all EAA, and high plasma levels of glycine, serine, urea and ammonia. In the lighter lambs, there were pronounced responses of PFAA levels to changes in the dietary proportion of EAA. At low proportions, the levels of most EAA in plasma were low. Lysine and phenylalanine were exceptions. In addition, levels of many non-essential amino acids (non-EAA), particularly serine and glycine, were high. At high proportions of EAA, plasma levels of all EAA, especially methionine, rose markedly. Within the non-EAA, serine, proline and glycine were reduced, while taurine and cystathionine increased. In the plasma of the heavier lambs, the response of some amino acids to a given dietary change differed from the response in the lighter lambs. This was especially true of methionine, tyrosine, phenylalanine and arginine. There was also marked between-animal variation in plasma levels. When expressed as molar proportions of total PFAA, results were similar to those of the lighter lambs. There was a pronounced similarity between the response of the PFAA to diets with a low proportion of EAA, and the PFAA pattern characteristic of developing kwashiorkor. __________________ *Part II, Aust. J. Agric. Res., 28, 933 (1977).

scholarly journals The Effect of Fermentation with Kefir Grains on the Physicochemical and Antioxidant Properties of Beverages from Blue Lupin (Lupinus angustifolius L.) Seeds

Molecules ◽  
2020 ◽  
Vol 25 (24) ◽  
pp. 5791
Author(s):  
Łukasz Łopusiewicz ◽  
Emilia Drozłowska ◽  
Paulina Trocer ◽  
Paweł Kwiatkowski ◽  
Artur Bartkowiak ◽  
...  
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Microbial Population ◽  
Antioxidant Properties ◽  
Lupinus Angustifolius ◽  
Kefir Grains ◽  
Antioxidant Properties Of Beverages ◽  
Hydrolysis Of ◽  
Free Radicals Scavenging

Plant derived fermented beverages have recently gained consumers’ interest, particularly due to their intrinsic functional properties and presence of beneficial microorganisms. Three variants containing 5%, 10%, and 15% (w/w) of sweet blue lupin (Lupinus angustifolius L. cv. “Boregine”) seeds were inoculated with kefir grains and incubated at 25 °C for 24 h. After processing, beverages were stored in refrigerated conditions (6 °C) for 21 days. Changes in microbial population, pH, bioactive compounds (polyphenolics, flavonoids, ascorbic acid), reducing sugars, and free amino acids were estimated. Additionally, viscosity, firmness, color, and free radicals scavenging properties were determined. Results showed that lactic acid bacteria as well as yeast were capable of growing well in the lupin matrix without any supplementation. During the process of refrigeration, the viability of the microorganisms was over the recommended minimum level for kefir products. Hydrolysis of polysaccharides as well as increase of free amino acids was observed. As a result of fermentation, the beverages showed excellent DPPH, ABTS+·, ·OH, and O2− radicals scavenging activities with a potential when considering diseases associated with oxidative stress. This beverages could be used as a new, non-dairy vehicle for beneficial microflora consumption, especially by vegans and lactose-intolerant consumers.

Dietary regulation of intestinal transport of the dipeptide carnosine

1988 ◽  
Vol 255 (2) ◽  
pp. G143-G150 ◽  
Author(s):  
R. P. Ferraris ◽  
J. Diamond ◽  
W. W. Kwan
Keyword(s):  
Amino Acids ◽  
Cell Surface ◽  
Dietary Protein ◽  
Free Amino Acids ◽  
Free Amino ◽  
Intestinal Transport ◽  
Dietary Regulation ◽  
Dietary Protein Level ◽  
Low Protein ◽  
Hydrolysis Of

Uptake of the dipeptide L-carnosine was measured in everted intestinal sleeves of mice whose dietary protein level or else proportion of protein in the form of free amino acids was varied experimentally. Carnosine uptake was highest in the jejunum, regardless of ration. Compared with a low-protein (18%) ration, a high-protein (72%) ration stimulated carnosine uptake by 30-70% in duodenum and jejunum (but not in ileum). This stimulation was observed even in the presence of peptidase inhibitors that inhibit cell surface hydrolysis of dipeptides. Measured carnosine hydrolysis was low or negligible. Carnosine uptake was the same in mice fed 54% unhydrolyzed casein, 54% partly hydrolyzed casein, and 54% free amino acids formulated so as to stimulate a complete hydrolysate of casein. Thus carnosine uptake is regulated by dietary levels of amino acids, peptides, and proteins, all of which seem equally effective at inducing carnosine transporters.

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