Utilization of amino acids as sole nitrogen sources by thermophilic fungi

In this paper we studied the effect of different amino acids (arginine, tryptophan, tyrosine, and phenylalanine) as nitrogen sources on the growth of actinomycete Streptomyces hygroscopicus CH-7 and the consumption of crude glycerol, obtained as a by-product in the biodiesel production from sunflower oil. The highest biomass concentration (9.5 g/L) was achieved using the basic medium and the medium with tryptophan (9.2 g/L), while the crude glycerol consumption was the highest in the basic medium (5.9 mg/mL) and the medium with phenylalanine (3.3 mg/mL).

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Production of single cell protein (SCP) and essentials amino acids from Candida utilis FMJ12 by solid state fermentation using mango waste supplemented with nitrogen sources

AFRICAN JOURNAL OF BIOTECHNOLOGY ◽

10.5897/ajb2017.16361 ◽

2018 ◽

Vol 17 (23) ◽

pp. 716-723 ◽

Cited By ~ 2

Author(s):

Kounbesioune SOMDA Marius ◽

NIKIEMA Mahamadi ◽

KEITA Ibrahim ◽

MOGMENGA Iliassou ◽

H. S. KOUHOUNDE Sonagnon ◽

...

Keyword(s):

Amino Acids ◽

Solid State ◽

Single Cell ◽

Solid State Fermentation ◽

Candida Utilis ◽

Nitrogen Sources ◽

Single Cell Protein ◽

Cell Protein

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Amino acid uptake systems in Bacteroides ruminicola

Canadian Journal of Microbiology ◽

10.1139/m79-180 ◽

1979 ◽

Vol 25 (10) ◽

pp. 1161-1168 ◽

Cited By ~ 15

Author(s):

Roselynn M. W. Stevenson

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Nitrogen Sources ◽

Amino Acid Uptake ◽

Defined Medium ◽

High Rate ◽

Transport Systems ◽

Acid Uptake ◽

Chemical Structures ◽

Kinetic Inhibition

Uptake of amino acids by Bacteroides ruminicola was observed in cells grown in a complete defined medium, containing ammonia as the nitrogen source. A high rate of uptake occurred only in fresh medium, as an inhibitory substance, possibly acetate, apparently accumulated during growth. All amino acids except proline were taken up and incorporated into cold trichloroacetic acid precipitable material. Different patterns of incorporation and different responses to 2,4-dinitrophenol and potassium ferricyanide indicated multiple uptake systems were involved. Kinetic inhibition patterns suggested six distinct systems were present for amino acid uptake, with specificities related to the chemical structures of the amino acids. Thus, the failure of free amino acids to act as sole nitrogen sources for growth of B. ruminicola is not due to the absence of transport systems for these compounds.

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Inhibiting Methanogenesis Stimulated de novo Synthesis of Microbial Amino Acids in Mixed Rumen Batch Cultures Growing on Starch but not on Cellulose

Microorganisms ◽

10.3390/microorganisms8060799 ◽

2020 ◽

Vol 8 (6) ◽

pp. 799

Author(s):

Emilio M. Ungerfeld ◽

M. Fernanda Aedo ◽

Camila Muñoz ◽

Natalie L. Urrutia ◽

Emilio D. Martínez ◽

...

Keyword(s):

Amino Acids ◽

De Novo ◽

Nitrogen Sources ◽

Environmental Benefits ◽

De Novo Synthesis ◽

Protein Nitrogen ◽

Protein Supplements ◽

Batch Cultures ◽

Sufficient Energy ◽

Ruminant Diets

Ameliorating methane (CH4) emissions from ruminants would have environmental benefits, but it is necessary to redirect metabolic hydrogen ([H]) toward useful sinks to also benefit animal productivity. We hypothesized that inhibiting rumen methanogenesis would increase de novo synthesis of microbial amino acids (AA) as an alternative [H] sink if sufficient energy and carbon are provided. We examined the effects of inhibiting methanogenesis with 9, 10-anthraquione (AQ) on mixed rumen batch cultures growing on cellulose or starch as sources of energy and carbon contrasting in fermentability, with ammonium (NH4+) or trypticase (Try) as nitrogen (N) sources. Inhibiting methanogenesis with AQ inhibited digestion with cellulose but not with starch, and decreased propionate and increased butyrate molar percentages with both substrates. Inhibiting methanogenesis with 9, 10-anthraquinone increased de novo synthesis of microbial AA with starch but not with cellulose. The decrease in the recovery of [H] caused by the inhibition of methanogenesis was more moderate with starch due to an enhancement of butyrate and AA as [H] sinks. There may be an opportunity to simultaneously decrease the emissions of CH4 and N with some ruminant diets and replace plant protein supplements with less expensive non-protein nitrogen sources such as urea.

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Growth and Plasma Amino Acids of Steers Fed Different Nitrogen Sources at Restricted Intake

Journal of Animal Science ◽

10.2527/jas1975.404714x ◽

1975 ◽

Vol 40 (4) ◽

pp. 714-719 ◽

Cited By ~ 7

Author(s):

W. R. Burris ◽

N. W. Bradley ◽

J. A. Boling

Keyword(s):

Amino Acids ◽

Nitrogen Sources ◽

Plasma Amino Acids

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THE IN VITRO RELEASE OF AMINO ACIDS BY RUMEN PAPILLAE

Canadian Journal of Animal Science ◽

10.4141/cjas80-037 ◽

1980 ◽

Vol 60 (2) ◽

pp. 281-291 ◽

Cited By ~ 2

Author(s):

R. J. BOILA ◽

L. P. MILLIGAN

Keyword(s):

Amino Acids ◽

Carbon Sources ◽

In Vitro Release ◽

Nitrogen Sources ◽

Chromatographic Technique ◽

Salts Of Organic Acids ◽

Liquid Chromatographic ◽

Vitro Release ◽

Effective Source

Rumen papillae from cattle were incubated aerobically with combinations of NH4Cl, amino acids and salts of organic acids, the latter including propionate, pyruvate, α-ketoglutarate and glyoxylate. Amino acids in the incubation media were analyzed using a gas-liquid chromatographic technique entailing separation of the isobutyl-N(0)-heptafluorobutyryl esters: glutamine was recovered with glutamate, asparagine with aspartate, and citrulline with ornithine. Rumen papillae incubated with pyruvate or propionate released alanine, but with the latter substrate only glutamate was effective as a nitrogen source. Glycine and glutamate plus glutamine were released in the presence of glyoxylate and α-ketoglutarate, respectively. Serine and aspartate plus asparagine were not quantitatively major products released by rumen papillae. Glutamate was an effective source of nitrogen for the release of alanine and glycine with pyruvate and glyoxylate, respectively, as carbon sources. When rumen papillae were incubated with pyruvate or glyoxylate as the added carbon source, glutamine nitrogen disappeared and was not accounted for by the amino acids measured. With arginine as a substrate, there was a release of ornithine by rumen papillae indicating urea production. The tissues of rumen papillae appear to synthesize amino acids from expected carbon sources with ammonia or glutamate as nitrogen sources and to catabolize glutamine and arginine. The metabolism of amino acids by rumen papillae would contribute to the interchange of nitrogen between the rumen and the host.

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An In Vitro TORC1 Kinase Assay That Recapitulates the Gtr-Independent Glutamine-Responsive TORC1 Activation Mechanism on Yeast Vacuoles

Molecular and Cellular Biology ◽

10.1128/mcb.00075-17 ◽

2017 ◽

Vol 37 (14) ◽

Cited By ~ 26

Author(s):

Mirai Tanigawa ◽

Tatsuya Maeda

Keyword(s):

Amino Acids ◽

Nitrogen Sources ◽

Small Gtpases ◽

Activation Mechanism ◽

Kinase Assay ◽

Content Type ◽

Vacuolar Protein ◽

Vacuolar Membranes ◽

First Time

ABSTRACT Evolutionarily conserved target of rapamycin (TOR) complex 1 (TORC1) responds to nutrients, especially amino acids, to promote cell growth. In the yeast Saccharomyces cerevisiae, various nitrogen sources activate TORC1 with different efficiencies, although the mechanism remains elusive. Leucine, and perhaps other amino acids, was reported to activate TORC1 via the heterodimeric small GTPases Gtr1-Gtr2, the orthologues of the mammalian Rag GTPases. More recently, an alternative Gtr-independent TORC1 activation mechanism that may respond to glutamine was reported, although its molecular mechanism is not clear. In studying the nutrient-responsive TORC1 activation mechanism, the lack of an in vitro assay hinders associating particular nutrient compounds with the TORC1 activation status, whereas no in vitro assay that shows nutrient responsiveness has been reported. In this study, we have developed a new in vitro TORC1 kinase assay that reproduces, for the first time, the nutrient-responsive TORC1 activation. This in vitro TORC1 assay recapitulates the previously predicted Gtr-independent glutamine-responsive TORC1 activation mechanism. Using this system, we found that this mechanism specifically responds to l-glutamine, resides on the vacuolar membranes, and involves a previously uncharacterized Vps34-Vps15 phosphatidylinositol (PI) 3-kinase complex and the PI-3-phosphate [PI(3)P]-binding FYVE domain-containing vacuolar protein Pib2. Thus, this system was proved to be useful for dissecting the glutamine-responsive TORC1 activation mechanism.

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EFFECT OF AMMONIUM NITROGEN AND AMINO ACIDS ON PERITHECIAL FORMATION OF VENTURIA INAEQUALIS

Canadian Journal of Plant Science ◽

10.4141/cjps71-006 ◽

1971 ◽

Vol 51 (1) ◽

pp. 29-33 ◽

Cited By ~ 5

Author(s):

R. G. ROSS ◽

FRANCES D. J. BREMNER

Keyword(s):

Amino Acids ◽

Ammonium Carbonate ◽

Venturia Inaequalis ◽

Amino Nitrogen ◽

Basal Medium ◽

Nitrogen Sources ◽

Ammonium Nitrogen ◽

Racemic Mixture ◽

Appreciable Change ◽

The Media

Perithecia of Venturia inaequalis did not form in a basal medium to which was added ammonium sulfate, chloride, phosphate or tartrate as the sole sources of nitrogen, when the pH of the medium was allowed to fall to inhibitory levels. Perithecia formed with these ammonium salts as nitrogen sources when calcium carbonate was added to control the pH. With ammonium carbonate and oxalate there was no appreciable change in pH, and perithecia formed with these salts as nitrogen sources. Perithecia did not form in media with leucine as a nitrogen source. Formation of perithecia with other amino acids depended on the concentration of amino-nitrogen in the media. A substance toxic to perithecial formation may form in cultures containing leucine; if so, it is produced in different amounts by the two isomers and the racemic mixture of this amino acid.

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