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1.
Electron. j. biotechnol ; Electron. j. biotechnol;35: 10-17, sept. 2018. tab, graf
Article de Anglais | LILACS | ID: biblio-1047827

RÉSUMÉ

Alanine mother liquor, a type of industrial waste from alanine fermentation, was used as a nitrogen source to produce docosahexaenoic acid (DHA) by Schizochytrium sp. B4D1. The results indicated that yeast extract could trigger the utilization of the alanine mother liquor. Additionally, the alanine can be quenched during the culture, which aids in DHA accumulation. The medium components were optimized via response surface methodology as follows: 99.98-g/L glucose, 0.05-g/L yeast extract and a 183.17 dilution factor of the alanine mother liquid (v/v, with an alanine content of 0.72 g/L) and 17.98% inoculum concentration (v/v). Finally, in a 50-mL shake-flask fermentation, the DHA yield was 2.29 g/L.


Sujet(s)
Acide docosahexaénoïque/biosynthèse , Alanine/métabolisme , Straménopiles/métabolisme , Levures , Protéines et peptides de signalisation intercellulaire/isolement et purification , Alanine/analyse , Fermentation , Glucose , Déchets industriels
2.
Electron. j. biotechnol ; Electron. j. biotechnol;30: 58-63, nov. 2017. ilus, tab, graf
Article de Anglais | LILACS | ID: biblio-1021458

RÉSUMÉ

Background: Mutation breeding is one of the most important routes to achieving high docosahexaenoic acid (DHA) productivity using Schizochytrium. However, few selection strategies have been reported that aim to generate a high DHA content in Schizochytrium lipids. Results: First, culture temperature altered the butanol tolerance of Schizochytrium limacinum B4D1. Second, S. limacinum E8 was obtained by selecting mutants with high butanol tolerance. This mutant exhibited a 17.97% lower proportion of DHA than the parent strain S. limacinum B4D1. Third, a negative selection strategy was designed in which S. limacinum F6, a mutant with poor butanol tolerance, was obtained. The proportion of DHA in S. limacinum F6 was 11.22% higher than that of parent strain S. limacinum B4D1. Finally, the performances of S. limacinum B4D1, E8 and F6 were compared. These three strains had different fatty acid profiles, but there was no statistical difference in their biomasses and lipid yields. Conclusion: It was feasible to identified the relative DHA content of S. limacinum mutants based on their butanol tolerance.


Sujet(s)
Acide docosahexaénoïque/biosynthèse , Butanols/métabolisme , Straménopiles/génétique , Straménopiles/métabolisme , Sélection génétique , Température , Acide eicosapentanoïque/métabolisme , Biomasse , Butanols/toxicité , Acides gras/métabolisme , Acides gras/composition chimique , Straménopiles/effets des médicaments et des substances chimiques , Fermentation , Mutation
3.
PLoS Pathog ; 9(10): e1003657, 2013.
Article de Anglais | MEDLINE | ID: mdl-24130481

RÉSUMÉ

Aquatic birds harbor diverse influenza A viruses and are a major viral reservoir in nature. The recent discovery of influenza viruses of a new H17N10 subtype in Central American fruit bats suggests that other New World species may similarly carry divergent influenza viruses. Using consensus degenerate RT-PCR, we identified a novel influenza A virus, designated as H18N11, in a flat-faced fruit bat (Artibeus planirostris) from Peru. Serologic studies with the recombinant H18 protein indicated that several Peruvian bat species were infected by this virus. Phylogenetic analyses demonstrate that, in some gene segments, New World bats harbor more influenza virus genetic diversity than all other mammalian and avian species combined, indicative of a long-standing host-virus association. Structural and functional analyses of the hemagglutinin and neuraminidase indicate that sialic acid is not a ligand for virus attachment nor a substrate for release, suggesting a unique mode of influenza A virus attachment and activation of membrane fusion for entry into host cells. Taken together, these findings indicate that bats constitute a potentially important and likely ancient reservoir for a diverse pool of influenza viruses.


Sujet(s)
Chiroptera/virologie , Réservoirs de maladies/virologie , Glycoprotéine hémagglutinine du virus influenza/génétique , Virus de la grippe A/génétique , Infections à Orthomyxoviridae/génétique , Phylogenèse , Animaux , Infections à Orthomyxoviridae/épidémiologie , Infections à Orthomyxoviridae/médecine vétérinaire , Pérou/épidémiologie
4.
Proc Natl Acad Sci U S A ; 109(11): 4269-74, 2012 Mar 13.
Article de Anglais | MEDLINE | ID: mdl-22371588

RÉSUMÉ

Influenza A virus reservoirs in animals have provided novel genetic elements leading to the emergence of global pandemics in humans. Most influenza A viruses circulate in waterfowl, but those that infect mammalian hosts are thought to pose the greatest risk for zoonotic spread to humans and the generation of pandemic or panzootic viruses. We have identified an influenza A virus from little yellow-shouldered bats captured at two locations in Guatemala. It is significantly divergent from known influenza A viruses. The HA of the bat virus was estimated to have diverged at roughly the same time as the known subtypes of HA and was designated as H17. The neuraminidase (NA) gene is highly divergent from all known influenza NAs, and the internal genes from the bat virus diverged from those of known influenza A viruses before the estimated divergence of the known influenza A internal gene lineages. Attempts to propagate this virus in cell cultures and chicken embryos were unsuccessful, suggesting distinct requirements compared with known influenza viruses. Despite its divergence from known influenza A viruses, the bat virus is compatible for genetic exchange with human influenza viruses in human cells, suggesting the potential capability for reassortment and contributions to new pandemic or panzootic influenza A viruses.


Sujet(s)
Chiroptera/virologie , Virus de la grippe A/génétique , Phylogenèse , Animaux , DNA-directed RNA polymerases/métabolisme , Gènes rapporteurs/génétique , Génome viral/génétique , Géographie , Guatemala , Glycoprotéine hémagglutinine du virus influenza/composition chimique , Glycoprotéine hémagglutinine du virus influenza/génétique , Humains , Données de séquences moléculaires , Sialidase/composition chimique , Sialidase/génétique , Analyse de séquence d'ADN
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