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1.
Food Chem ; 135(4): 2575-83, 2012 Dec 15.
Artigo em Inglês | MEDLINE | ID: mdl-22980845

RESUMO

Coffee grown at high elevations fetches a better price than that grown in lowland regions. This study was aimed at determining whether climatic conditions during bean development affected sensory perception of the coffee beverage and combinations of volatile compounds in green coffee. Green coffee samples from 16 plots representative of the broad range of climatic variations in Réunion Island were compared by sensory analysis. Volatiles were extracted by solid phase micro-extraction and the volatile compounds were analysed by GC-MS. The results revealed that, among the climatic factors, the mean air temperature during seed development greatly influenced the sensory profile. Positive quality attributes such as acidity, fruity character and flavour quality were correlated and typical of coffees produced at cool climates. Two volatile compounds (ethanal and acetone) were identified as indicators of these cool temperatures. Among detected volatiles, most of the alcohols, aldehydes, hydrocarbons and ketones appeared to be positively linked to elevated temperatures and high solar radiation, while the sensory profiles displayed major defects (i.e. green, earthy flavour). Two alcohols (butan-1,3-diol and butan-2,3-diol) were closely correlated with a reduction in aromatic quality, acidity and an increase in earthy and green flavours. We assumed that high temperatures induce accumulation of these compounds in green coffee, and would be detected as off-flavours, even after roasting. Climate change, which generally involves a substantial increase in average temperatures in mountainous tropical regions, could be expected to have a negative impact on coffee quality.


Assuntos
Coffea/química , Café/química , Odorantes/análise , Compostos Orgânicos Voláteis/análise , Clima , Coffea/crescimento & desenvolvimento , Coffea/metabolismo , Café/normas , Ecossistema , Humanos , Controle de Qualidade , Paladar , Compostos Orgânicos Voláteis/metabolismo
2.
Expert Opin Ther Targets ; 7(5): 593-602, 2003 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-14498822

RESUMO

Chemotherapy of malaria parasites is limited by established drug resistance and lack of novel treatment options. Intraerythrocytic stages of Plasmodium falciparum, the causative agent of severe malaria, are wholly dependent upon host glucose for energy. A facilitative hexose transporter (PfHT), encoded by a single-copy gene, mediates glucose uptake and is therefore an attractive potential target. The authors first established heterologous expression in Xenopus laevis to allow functional characterisation of PfHT. They then used this expression system to compare the interaction of substrates with PfHT and mammalian Gluts (hexose transporters) and identified important differences between host and parasite transporters. Certain Omethyl derivatives of glucose proved to be particularly useful discriminators between mammalian transporters and PfHT. The authors exploited this selectivity and synthesised an O-3 hexose derivative that potently inhibits PfHT expressed in oocytes. This O-3 derivative (compound 3361) also kills cultured P. falciparum with comparable potency. Compound 3361 acts with reasonable specificity against PfHT orthologues encoded by other parasites such as Plasmodium vivax, Plasmodium yoelii and Plasmodium knowlesi. Multiplication of Plasmodium berghei in a mouse model is also significantly impeded by this compound. These findings validate PfHT as a novel target.


Assuntos
Antimaláricos/farmacologia , Desenho de Fármacos , Glucose/análogos & derivados , Malária Falciparum/tratamento farmacológico , Proteínas de Transporte de Monossacarídeos/antagonistas & inibidores , Plasmodium falciparum/efeitos dos fármacos , Proteínas de Protozoários/antagonistas & inibidores , Sequência de Aminoácidos , Animais , Antimaláricos/uso terapêutico , Avaliação Pré-Clínica de Medicamentos , Metabolismo Energético/efeitos dos fármacos , Fermentação , Frutose/metabolismo , Regulação da Expressão Gênica , Glucose/química , Glucose/metabolismo , Glicólise/efeitos dos fármacos , Humanos , Malária Falciparum/parasitologia , Mamíferos/metabolismo , Camundongos , Dados de Sequência Molecular , Proteínas de Transporte de Monossacarídeos/genética , Proteínas de Transporte de Monossacarídeos/fisiologia , Mutagênese Sítio-Dirigida , Plasmodium/efeitos dos fármacos , Plasmodium/enzimologia , Plasmodium falciparum/enzimologia , Plasmodium falciparum/genética , Plasmodium falciparum/crescimento & desenvolvimento , Proteínas de Protozoários/genética , Proteínas de Protozoários/fisiologia , Proteínas Recombinantes de Fusão/antagonistas & inibidores , Alinhamento de Sequência , Homologia de Sequência de Aminoácidos , Especificidade da Espécie , Relação Estrutura-Atividade , Especificidade por Substrato , Xenopus laevis
3.
Appl Microbiol Biotechnol ; 60(1-2): 114-9, 2002 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-12382051

RESUMO

Seeds of the tropical tree Moringa oleifera contain small storage proteins able to flocculate particles in suspension in water. The cDNA encoding one of these flocculent proteins, MO(2.1), was cloned and the recombinant protein was expressed in Escherichia coli. The flocculent activity of the purified recombinant MO(2.1)was assayed on clays and bacteria using light and confocal microscopy and GFP-overexpressing bacteria. We show that MO(2.1)is able to aggregate montmorillonite clay particles as well as gram-positive and gram-negative bacteria. We discuss the use of recombinant proteins to study flocculating properties and improve water purification processes.


Assuntos
Bactérias Gram-Negativas/efeitos dos fármacos , Bactérias Gram-Positivas/efeitos dos fármacos , Moringa oleifera/química , Proteínas de Plantas/química , Proteínas de Plantas/farmacologia , Sementes/química , Sequência de Aminoácidos , Sequência de Bases , Clonagem Molecular , Escherichia coli , Floculação , Bactérias Gram-Negativas/ultraestrutura , Bactérias Gram-Positivas/ultraestrutura , Microscopia Confocal , Dados de Sequência Molecular , Proteínas de Plantas/genética , Proteínas de Plantas/isolamento & purificação , Proteínas Recombinantes/química , Análise de Sequência
4.
Plant Physiol ; 125(4): 1919-29, 2001 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-11299371

RESUMO

Tobacco (Nicotiana tabacum var Petit Havana) ndhB-inactivated mutants (ndhB-) obtained by plastid transformation (E.M. Horvath, S.O. Peter, T. Joët, D. Rumeau, L. Cournac, G.V. Horvath, T.A. Kavanagh, C. Schäfer, G. Peltier, P. MedgyesyHorvath [2000] Plant Physiol 123: 1337-1350) were used to study the role of the NADH-dehydrogenase complex (NDH) during photosynthesis and particularly the involvement of this complex in cyclic electron flow around photosystem I (PSI). Photosynthetic activity was determined on leaf discs by measuring CO2 exchange and chlorophyll fluorescence quenchings during a dark-to-light transition. In the absence of treatment, both non-photochemical and photochemical fluorescence quenchings were similar in ndhB- and wild type (WT). When leaf discs were treated with 5 microM antimycin A, an inhibitor of cyclic electron flow around PSI, both quenchings were strongly affected. At steady state, maximum photosynthetic electron transport activity was inhibited by 20% in WT and by 50% in ndhB-. Under non-photorespiratory conditions (2% O2, 2,500 microL x L(-1) CO2), antimycin A had no effect on photosynthetic activity of WT, whereas a 30% inhibition was observed both on quantum yield of photosynthesis assayed by chlorophyll fluorescence and on CO2 assimilation in ndhB-. The effect of antimycin A on ndhB- could not be mimicked by myxothiazol, an inhibitor of the mitochondrial cytochrome bc1 complex, therefore showing that it is not related to an inhibition of the mitochondrial electron transport chain but rather to an inhibition of cyclic electron flow around PSI. We conclude to the existence of two different pathways of cyclic electron flow operating around PSI in higher plant chloroplasts. One of these pathways, sensitive to antimycin A, probably involves ferredoxin plastoquinone reductase, whereas the other involves the NDH complex. The absence of visible phenotype in ndhB- plants under normal conditions is explained by the complement of these two pathways in the supply of extra-ATP for photosynthesis.


Assuntos
Antimicina A/farmacologia , NADH Desidrogenase/metabolismo , Nicotiana/fisiologia , Fotossíntese/fisiologia , Complexo de Proteínas do Centro de Reação Fotossintética/metabolismo , Proteínas de Plantas/genética , Plantas Tóxicas , Dióxido de Carbono/metabolismo , Clorofila/metabolismo , Transporte de Elétrons , Cinética , Luz , Complexos de Proteínas Captadores de Luz , Metacrilatos , Fotossíntese/efeitos dos fármacos , Complexo de Proteína do Fotossistema I , Plastídeos/genética , Tiazóis/farmacologia , Nicotiana/efeitos dos fármacos , Nicotiana/genética
5.
Philos Trans R Soc Lond B Biol Sci ; 355(1402): 1447-54, 2000 Oct 29.
Artigo em Inglês | MEDLINE | ID: mdl-11127998

RESUMO

Besides electron transfer reactions involved in the 'Z' scheme of photosynthesis, alternative electron transfer pathways have been characterized in chloroplasts. These include cyclic electron flow around photosystem I (PS I) or a respiratory chain called chlororespiration. Recent work has supplied new information concerning the molecular nature of the electron carriers involved in the non-photochemical reduction of the plastoquinone (PQ) pool. However, until now little is known concerning the nature of the electron carriers involved in PQ oxidation. By using mass spectrometric measurement of oxygen exchange performed in the presence of 18O-enriched O2 and Chlamydomonas mutants deficient in PS I, we show that electrons can be directed to a quinol oxidase sensitive to propyl gallate but insensitive to salicyl hydroxamic acid. This oxidase has immunological and pharmacological similarities with a plastid protein involved in carotenoid biosynthesis.


Assuntos
Cloroplastos/enzimologia , Complexos de Proteínas Captadores de Luz , Oxirredutases/metabolismo , Fotossíntese/fisiologia , Complexo de Proteínas do Centro de Reação Fotossintética/metabolismo , Complexo de Proteína do Fotossistema I , Tilacoides/metabolismo , Animais , Respiração Celular , Chlamydomonas reinhardtii/metabolismo , Cloroplastos/metabolismo , Grupo dos Citocromos b/metabolismo , Complexo Citocromos b6f , Transporte de Elétrons , Proteínas de Membrana/genética , Proteínas de Membrana/fisiologia , Oxigênio/metabolismo , Complexo de Proteínas do Centro de Reação Fotossintética/genética , Proteínas de Plantas/genética , Proteínas de Plantas/fisiologia
6.
Plant Physiol ; 123(4): 1337-50, 2000 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-10938352

RESUMO

The ndh genes encoding for the subunits of NAD(P)H dehydrogenase complex represent the largest family of plastid genes without a clearly defined function. Tobacco (Nicotiana tabacum) plastid transformants were produced in which the ndhB gene was inactivated by replacing it with a mutant version possessing translational stops in the coding region. Western-blot analysis indicated that no functional NAD(P)H dehydrogenase complex can be assembled in the plastid transformants. Chlorophyll fluorescence measurements showed that dark reduction of the plastoquinone pool by stromal reductants was impaired in ndhB-inactivated plants. Both the phenotype and photosynthetic performance of the plastid transformants was completely normal under favorable conditions. However, an enhanced growth retardation of ndhB-inactivated plants was revealed under humidity stress conditions causing a moderate decline in photosynthesis via stomatal closure. This distinctive phenotype was mimicked under normal humidity by spraying plants with abscisic acid. Measurements of CO(2) fixation demonstrated an enhanced decline in photosynthesis in the mutant plants under humidity stress, which could be restored to wild-type levels by elevating the external CO(2) concentration. These results suggest that the plastid NAD(P)H:plastoquinone oxidoreductase in tobacco performs a significant physiological role by facilitating photosynthesis at moderate CO(2) limitation.


Assuntos
Inativação Gênica , NADPH Desidrogenase/metabolismo , Nicotiana/metabolismo , Fotossíntese , Proteínas de Plantas/metabolismo , Plantas Tóxicas , Plastídeos/metabolismo , Ácido Abscísico/metabolismo , Ácido Abscísico/farmacologia , Sequência de Bases , Western Blotting , Dióxido de Carbono/metabolismo , Umidade , Dados de Sequência Molecular , NADPH Desidrogenase/genética , Oxigênio/metabolismo , Fenótipo , Folhas de Planta/genética , Folhas de Planta/metabolismo , Proteínas de Plantas/genética , Plastídeos/genética , Nicotiana/genética , Nicotiana/crescimento & desenvolvimento
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