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Growth and luminescence of luminous bacteria promoted by agents of microbial origin. / E. K. Rodicheva [et al.] // Journal of bioluminescence and chemiluminescence. - 1993. - Vol. 8, Is. 6. - P293-299 . - ISSN 0884-3996
Кл.слова (ненормированные):
amino acid -- carbohydrate -- folic acid -- luciferase -- nitrogen -- riboflavin -- article -- biosynthesis -- culture medium -- electron microscopy -- growth, development and aging -- kinetics -- luminescence -- metabolism -- Photobacterium -- physiology -- time -- ultrastructure -- Vibrio -- Amino Acids -- Carbohydrates -- Culture Media -- Folic Acid -- Kinetics -- Luciferase -- Luminescence -- Microscopy, Electron -- Nitrogen -- Photobacterium -- Riboflavin -- Time Factors -- Vibrio
Аннотация: The examination of four species of luminous bacteria Photobacterium leiognathi, Photobacterium phosphoreum, Vibrio fischeri and Vibrio harveyi has enabled us to reveal some nutrient medium components effecting growth, luminescence intensity and luciferase synthesis. These agents are nucleic components (nucleotides, nucleotides and amine bases), amino acids and vitamins, which are part of hydrolysates from the biomass of various lithotrophic microorganisms, hydrogen-oxidizing, iron-oxidizing and carboxydobacteria. The effect of promoting agents essentially alters the physiological state and ultrastructure of the cells of luminous bacteria and increases luciferase biosynthesis two- to three-fold compared to a control.

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Держатели документа:
Institute of Biophysics, Russian Academy of Sciences, Krasnoyarsk. : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Rodicheva, E.K.; Trubachev, I.N.; Medvedeva, S.E.; Egorova, O.I.; , U - Shitova LYu

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Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8-ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria / V. N. Petushkov [et al.] // Journal of Physical Chemistry B. - 2003. - Vol. 107, Is. 39. - P10934-10939 . - ISSN 1520-6106
Кл.слова (ненормированные):
Bacteria -- Bioluminescence -- Chemical relaxation -- Chromophores -- Dielectric properties -- Proteins -- Solvents -- Bioluminescent bacteria -- Dimethyl ribityl lumazine -- Photobacterium leiognathi -- Riboflavin -- Ultrafast fluorescence relaxation spectroscopy -- Fluorescence
Аннотация: The solvation dynamics of interesting bioluminescent chromophores have been determined, using subpicosecond and wavelength-resolved fluorescence spectroscopy, in combination with global analysis of the multidimensional data sets. The systems investigated comprise the free ligands 6,7-dimethyl-(8-ribityl)-lumazine (lumazine) and riboflavin in an aqueous buffer and both ligands when noncovalently bound to two bacterial bioluminescent antenna proteins: lumazine protein (from Photobacterium leiognathi) and the blue fluorescent protein (from Vibrio fischeri Y1). Fluorescence spectral relaxation of the free ligands is complete within a few picoseconds. Subsequently, the fluorescence intensity increases by ?7% on a time scale of 15-30 ps. Fluorescence spectral relaxation of the protein-bound ligands is largely complete within 1 ps but reveals a small red shift with a minor, but distinctly longer, relaxation time than that of the free ligands, which is tentatively assigned to the relaxation of protein-bound water in the vicinity of the excited chromophore.

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Держатели документа:
MicroSpectroscopy Centre, Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, Netherlands
Department of Physics and Astronomy, Faculty of Sciences, Vrije Universiteit, De Boelelaan 1081, 1081 HV Amsterdam, Netherlands
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA 30602, United States
Department of Structural Biology, Faculty of Earth and Life Sciences, Vrije Universiteit, De Boelelaan 1087, 1081 HV Amsterdam, Netherlands
Institute of Biophysics, Academy of Sciences of Russia, Krasnoyarsk 660036, Russian Federation
IPMC, Universite de Lausanne, CH 1015 Lausanne, Switzerland : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Van Stokkum, I.H.M.; Gobets, B.; Van Mourik, F.; Lee, J.; Van Grondelle, R.; Visser, A.J.W.G.

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Properties of recombinant fluorescent proteins from Photobacterium leiognathi and their interaction with luciferase intermediates / V. N. Petushkov, B. G. Gibson, J. Lee // Biochemistry. - 1995. - Vol. 34, Is. 10. - P3300-3309 . - ISSN 0006-2960
Кл.слова (ненормированные):
luciferase -- recombinant protein -- article -- ligand binding -- nonhuman -- priority journal -- protein isolation -- protein protein interaction -- protein stability -- vibrionaceae -- Bacterial Proteins -- Binding Sites -- Carrier Proteins -- Circular Dichroism -- Flavin Mononucleotide -- Fluorescence Polarization -- Genes, Bacterial -- Kinetics -- Ligands -- Luciferase -- Luminescence -- Molecular Sequence Data -- Photobacterium -- Recombinant Proteins -- Spectrophotometry -- Support, U.S. Gov't, P.H.S. -- Photobacterium leiognathi -- Vibrionaceae
Аннотация: Ligand binding and luciferase interaction properties of the recombinant protein corresponding to the lumazine protein gene (EMBL X56534) of Photobacterium leiognathi have been determined by fluorescence dynamics, circular dichroism, gel filtration, and SDS-PAGE. Scatchard analysis of a fluorescence titration shows that the apoprotein possess one binding site, and at 30В°C the KdS (?M) are as follows: 6,7-dimethyl-8-ribityllumazine, 0.26; riboflavin, 0.53; and much more weakly bound FMN, 30. All holoproteins are highly fluorescent and have absorption spectra distinct from each other and from the free ligands. The longest wavelength absorption maxima are, respectively (nm, 2В°C), 420,463, and 458. Ligand binding produces no change in the far-UV circular dichroism; all have mean residual ellipticity at 210 nm of -6500 deg cm2 dmol-1, the same as the native protein. However, in the bioluminescence reaction only the lumazine holoprotein shows a bioluminescence effect. Fluorescence emission anisotropy decay was used to establish that none of these holoproteins complexed with native luciferase and that the lumazine protein alone formed a 1:1 complex with the luciferase hydroxyflavin fluorescent transient and the luciferase peroxyflavin intermediates, revealed by a dominant channel of anisotropy loss, with rotational correlation time of 2.5 ns, and attributed to excitation transfer from the luciferase flavin donor to the acceptor, the lumazine ligand. The complex stability was sufficient to allow its isolation by FPLC gel filtration and verification by SDS-PAGE. These methods also confirmed the absence of interaction of the holoflavoproteins.

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Держатели документа:
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, United States
Institute of Biophysics, Academy of Sciences of Russia (Siberian Branch), 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Gibson, B.G.; Lee, J.

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The yellow bioluminescence bacterium, Vibrio fischeri Y1, contains a bioluminescence active riboflavin protein in addition to the yellow fluorescence FMN protein / V. N. Petushkov, B. G. Gibson, J. Lee // Biochemical and Biophysical Research Communications. - 1995. - Vol. 211, Is. 3. - P774-779, DOI 10.1006/bbrc.1995.1880 . - ISSN 0006-291X
Кл.слова (ненормированные):
riboflavin -- article -- bioluminescence -- fluorescence -- nonhuman -- priority journal -- protein analysis -- protein synthesis -- vibrio -- vibrionaceae -- Bacterial Proteins -- Chromatography, Gel -- Chromatography, Thin Layer -- Flavin Mononucleotide -- Flavoproteins -- Luminescence -- Riboflavin -- Spectrometry, Fluorescence -- Support, U.S. Gov't, P.H.S. -- Vibrio -- Bacteria (microorganisms) -- Photobacterium -- Vibrio -- Vibrio fischeri
Аннотация: The yellow bioluminescence Y1 strain of Vibrio fischeri can produce a 22 kDa protein with either FMN or riboflavin as a bound fluorophore. Both forms are active for shifting the bioluminescence spectral maximum. The fluorescence spectral distribution of the two proteins differs slightly and the in vivo emission appears to be an equal mixture of the two. The bioluminescence activity of the riboflavin Y1 protein contrasts with the inactivity of the related Photobacterium type.

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Держатели документа:
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, United States
Institute of Biophysics, Academy of Sciences of Russia (Siberian Branch), 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Gibson, B.G.; Lee, J.

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Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1 / V. N. Petushkov, J. Lee // European Journal of Biochemistry. - 1997. - Vol. 245, Is. 3. - P790-796 . - ISSN 0014-2956
Кл.слова (ненормированные):
anisotropy -- lumazine protein -- Photobacterium -- thioredoxin reductase -- time-resolved fluorescence -- cytochrome -- flavoprotein -- article -- bioluminescence -- nonhuman -- priority journal -- protein analysis -- protein purification -- sea -- vibrio -- Amino Acid Sequence -- Bacterial Proteins -- Cytochromes -- Flavoproteins -- Molecular Sequence Data -- Sequence Alignment -- Vibrio -- Azotobacter -- Bacteria (microorganisms) -- Escherichia coli -- Haemophilus -- haemophilus influenza -- Murinae -- Negibacteria -- Photobacterium -- Photobacterium leiognathi -- Pseudomonas -- uncultured marine bacterium -- Vibrio fischeri
Аннотация: Several flavoproteins and cytochromes that occur as major components in extracts of the yellow bioluminescence Y1 strain of the murine bacterium Vibrio fischeri have been purified and characterized with respect to their mass (SDS/PAGE) and matrix-assisted laser-desorption/ionization MS), chromatographic properties, N-terminal sequence, and spectroscopy (absorption, fluorescence emission and anisotropy decay). The investigated proteins were as follows: yellow fluorescence protein (YFP) with bound riboflavin, FMN or 6,7-dimethyl-8-ribityllumazine; a blue fluorescence protein (BFP) with bound 6,7-dimethyl-8-ribityllumazine, riboflavin, or 6- methyl-7-oxo-ribityllumazine; thioredoxin reductase with FAD as ligand; and two c-type diheme cytochromes, c551 and c554. We present evidence that the riboflavin-bound YFP has an N-terminal sequence corresponding to that published for the dimeric YFP. We show that an equilibrium replacement of the riboflavin can be made with excess lumazine derivative and that lumazine- bound YFP has different bioluminescence properties to those of the lumazine protein from Photobacterium leiognathi. BFP is a different protein again, and in the bacterial lysate it occurs in multiple forms, ligated to either riboflavin, lumazine, or t he 7-oxolumazine derivative. The N-terminal sequence for BFP-shows similarities to those of the YFP proteins and to lumazine protein and riboflavin synthase from Photobacterium. BFP in any form has no bioluminescence or riboflavin-synthase activity. A 70-kDa fluorescent flavoprotein with FAD as ligand has an N-terminal sequence highly similar to those of thioredoxin reductases from Haemophilus influenza and Escherichia coli. Cytochrome contaminations in previous preparations of YFP have been removed and an identified as the two c-type cytochromes c551 and c554. Both inhibit the NADH-induced bioluminescence in the reductase/luciferase system with the luciferase from P. leiognathi and V. fischeri. The N-terminal amino acid sequence of the cytochrome (c551) corresponds to a diheme cytochrome c4. The spectral properties of c554 are similar to those of other c5 cytochromes, and both c554 and c551 have absorption spectra similar to those of the respective cytochromes from the gram-negative bacteria Pseudomonas and Azotobacter.

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Держатели документа:
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA, United States
Institute of Biophysics, Academy of Sciences of Russia, Krasnoyarsk, Russian Federation
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA 30602, United States : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Lee, J.

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Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (Antenna) proteins: Bioluminescence effects of the aliphatic additive [Text] / V. N. Petushkov [et al.] // Biochemistry. - 1996. - Vol. 35, Is. 37. - P12086-12093, DOI 10.1021/bi9608931. - Cited References: 41 . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
BACTERIAL LUCIFERASE
   LUMAZINE PROTEIN
   FLAVIN INTERMEDIATE
   ANGSTROM RESOLUTION
   RIBOFLAVIN PROTEIN
   PURIFICATION
   MECHANISM
   EMISSION
   ALDEHYDE
   INHIBITION
Аннотация: The kinetics of the bacterial bioluminescence reaction is altered in the presence of the fluorescent (antenna) proteins, lumazine protein (LumP) from Photobacterium or the yellow fluorescence proteins (YFP) having FMN or Rf bound, from Vibrio fischeri strain Y1, Depending on reaction conditions, the bioluminescence intensity and its decay rate may be either enhanced or strongly quenched in the presence of the fluorescent proteins. These effects call be simply explained on the basis of the same protein-protein complex model that accounts for the bioluminescence spectral shifts induced by these fluorescent proteins. In such a complex, when the fluorophore evidently is in proximity to the luciferase active site, it is expected that the on-off rate of certain aliphatic components of the reaction should be altered with a consequent shift in the equilibria among the luciferase intermediates, as recently elaborated in a kinetic scheme, These aliphatic components are the bioluminescence reaction substrate, tetradecanal or other long-chain aldehyde, its carboxylic acid product, or dodecanol used as a stabilizer of the luciferase peroxyflavin. No evidence can be found or the protein-protein interaction in the absence of the aliphatic component.

Держатели документа:
UNIV GEORGIA,DEPT BIOCHEM & MOL BIOL,ATHENS,GA 30602
RUSSIAN ACAD SCI,INST BIOPHYS,SIBERIAN BRANCH,KRASNOYARSK 660036,RUSSIA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Ketelaars, M...; Gibson, B.G.; Lee, J...

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Direct measurement of excitation transfer in the protein complex of bacterial luciferase hydroxyflavin and the associated yellow fluorescence proteins from Vibrio fischeri Y1 [Text] / V. N. Petushkov, B. G. Gibson, J. . Lee // Biochemistry. - 1996. - Vol. 35, Is. 25. - P8413-8418, DOI 10.1021/bi952691v. - Cited References: 24 . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
LUMAZINE PROTEIN
   LUMINOUS BACTERIUM
   STRAIN Y-1
   BIOLUMINESCENCE
   EMISSION
   PURIFICATION
   TRANSIENT
   LIGHT
Аннотация: Time-resolved fluorescence was used to directly measure the energy transfer rate constant in the protein-protein complex involved in the yellow bioluminescence of Vibrio fischeri, strain Y1. In this reaction the putative donor is the fluorescent transient intermediate, luciferase hydroxyflavin, which exhibits a major fluorescence lifetime of the bound flavin of 10 ns. On addition of the acceptor, the V. fischeri yellow fluorescence protein containing either FMN or riboflavin as ligand, a rapid decay time, 0.25 ns, becomes predominant. The same results are observed using rec-luciferase from Photobacterium leiognathi to produce the donor. Because of favorable spectral separation in this system, this rapid decay rate of 4 ns(-1), can be directly equated to the energy transfer rate. This rate is ten times higher than the rate previously observed in the Photobacterium luciferase hydroxyflavin-lumazine protein, donor-acceptor system, derived from emission anisotropy measurements. This ten-times ratio is close to the ratio of spectral overlaps of the donor fluorescence with the acceptor absorption, between these two systems, so it is concluded that the topology of the protein complexes in both cases, must be very similar. Energy transfer is also monitored by the loss of steady-state fluorescence intensity at 460 nm of the donor, on addition of the acceptor protein. A fluorescence titration indicates that luciferase hydroxyflavin and the yellow protein complex with a 1:1 stoichiometry with a K-d of 0.7 mu M (0 degrees C). These parameters account for the bioluminescence spectral shifting effects observed in these reactions.

Держатели документа:
UNIV GEORGIA,DEPT BIOCHEM & MOLEC BIOL,ATHENS,GA 30602
RUSSIAN ACAD SCI,INST BIOPHYS,SIBERIAN BRANCH,KRASNOYARSK 660036,RUSSIA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Gibson, B.G.; Lee, J...

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Purification and ligand exchange protocols for antenna proteins from bioluminescent bacteria [Text] / V. N. Petrushkov [et al.] // Methods Enzymol. - 2000. - Vol. 305. - P. 164-180. - Cited References: 18 . - ISSN 0076-6879

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology
Рубрики:
YELLOW FLUORESCENT PROTEIN
   FISCHERI STRAIN Y-1
   AMINO-ACID-SEQUENCE
   VIBRIO-FISCHERI
   PHOTOBACTERIUM-LEIOGNATHI
   RIBOFLAVIN PROTEIN
   LUMINOUS BACTERIUM
   LUMAZINE PROTEIN
   FMN
   Y1

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Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Agr Univ Wageningen, Dept Biochem, NL-6703 HA Wageningen, Netherlands
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petrushkov, V.N.; Gibson, B.G.; Visser, AJWG; Lee, J...

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Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8-ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria [Text] / V. N. Petushkov [et al.] // J. Phys. Chem. B. - 2003. - Vol. 107, Is. 39. - P. 10934-10939, DOI 10.1021/jp034266e. - Cited References: 52 . - ISSN 1520-6106

РУБ Chemistry, Physical
Рубрики:
TIME-RESOLVED FLUORESCENCE
   VIBRIO-FISCHERI Y1
   FEMTOSECOND SOLVATION DYNAMICS
   FLAVIN ADENINE-DINUCLEOTIDE
   PHOTOBACTERIUM-LEIOGNATHI
   BIOLOGICAL WATER
   SOLVENT DYNAMICS
   DIELECTRIC-RELAXATION
   MOLECULAR-DYNAMICS
   TRYPTOPHAN
Аннотация: The solvation dynamics of interesting bioluminescent chromophores have been determined, using subpicosecond and wavelength-resolved fluorescence spectroscopy, in combination with global analysis of the multidimensional data sets. The systems investigated comprise the free ligands 6,7-dimethyl-(8-ribityl)-lumazine (lumazine) and riboflavin in an aqueous buffer and both ligands when noncovalently bound to two bacterial bioluminescent antenna proteins: lumazine protein (from Photobacterium leiognathi) and the blue fluorescent protein (from Vibrio fischeri Y1). Fluorescence spectral relaxation of the free ligands is complete within a few picoseconds. Subsequently, the fluorescence intensity increases by similar to7% on a time scale of 15-30 ps. Fluorescence spectral relaxation of the protein-bound ligands is largely complete within 1 ps but reveals a small red shift with a minor, but distinctly longer, relaxation time than that of the free ligands, which is tentatively assigned to the relaxation of protein-bound water in the vicinity of the excited chromophore.

WOS
Держатели документа:
Univ Wageningen & Res Ctr, Biochem & Biophys Lab, MicroSpect Ctr, NL-6703 HA Wageningen, Netherlands
Vrije Univ Amsterdam, Fac Sci & Engn, Dept Phys & Astron, NL-1081 HV Amsterdam, Netherlands
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Vrije Univ Amsterdam, Fac Earth & Life Sci, Dept Biol Struct, NL-1081 HV Amsterdam, Netherlands
Russian Acad Sci, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; van Stokkum, IHM; Gobets, B...; van Mourik, F...; Lee, J...; van Grondelle, R...; Visser, AJWG

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10.

Computing-feasibility study of NASA nutrition requirements as applied to a bioregenerative life support system / V. S. Kovalev, N. S. Manukovsky, A. A. Tikhomirov // Acta Astronaut. - 2019. - Vol. 159. - P371-376, DOI 10.1016/j.actaastro.2019.04.001 . - ISSN 0094-5765
Кл.слова (ненормированные):
Constraint -- Food -- Modeling -- Nutrient -- Objective function -- Amino acids -- Animals -- Food products -- Models -- NASA -- Nutrients -- Nutrition -- Proteins -- Saturated fatty acids -- Uncertainty analysis -- Vitamins -- Bioregenerative life support systems -- Constraint -- Essential amino acids -- Independent variables -- Interpretation of models -- Long duration missions -- Lower and upper bounds -- Objective functions -- Life support systems (spacecraft)
Аннотация: In view of previous studies, a list of 46 foods designated for use in bioregenerative life support system was composed. With the help of a computer program, daily sets of foods of plant and animal origin were compiled from the list of foods. The objective function of modeling was intended to minimize the discrepancy between the calculated values of nutrients in daily food sets and NASA nutrition requirements for long-duration missions. The independent variables in the model were the masses of foods restricted by the lower and upper bounds. It was established that a food set is able to comprise 10-46 foods with violation of the NASA nutrition requirements for iron, vitamin B5 and vitamin D daily intakes. Inclusion of 9 foods in a set resulted in a further violation of the NASA standards concerning saturated fat. As the number of foods in a set has increased from 10 to 22, the objective function decreased from 1.0736 to 1.0332, followed by a gradual increase to 1.1233, when the maximum number of foods was selected from the list of foods. The source of uncertainty in the interpretation of modeling results are the standard NASA intakes of magnesium, potassium, zinc, manganese, vitamin C, thiamin, riboflavin, niacin, vitamin B6, folate, vitamin B12, vitamin E, vitamin K and n-6 fatty acids, given as exact values. Varying the nutrient content of food sets did not significantly affect the value of the objective function. However, some solutions were infeasible, due to the violation of the NASA standard concerning saturated fat. Also, there were food sets in which the scores of sulfur-containing amino acids and threonine were below 100. In order to reliably maintain the scores of essential amino acids above 100 in a food set, it is necessary to maintain a mass ratio of “animal protein/total protein” equal to 2/3 in accordance with the requirement of NASA. © 2019 IAA

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Держатели документа:
Institute of Biophysics of Siberian Branch of Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Kovalev, V. S.; Manukovsky, N. S.; Tikhomirov, A. A.

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