Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 10 de 10
Filtrar
Mais filtros










Base de dados
Intervalo de ano de publicação
1.
PLoS One ; 9(9): e105634, 2014.
Artigo em Inglês | MEDLINE | ID: mdl-25244522

RESUMO

Defining the specific role of the factors that affect metaphor processing is a fundamental step for fully understanding figurative language comprehension, either in discourse and conversation or in reading poems and novels. This study extends the currently available materials on everyday metaphorical expressions by providing the first dataset of metaphors extracted from literary texts and scored for the major psycholinguistic variables, considering also the effect of context. A set of 115 Italian literary metaphors presented in isolation (Experiment 1) and a subset of 65 literary metaphors embedded in their original texts (Experiment 2) were rated on several dimensions (word and phrase frequency, readability, cloze probability, familiarity, concreteness, difficulty and meaningfulness). Overall, literary metaphors scored around medium-low values on all dimensions in both experiments. Collected data were subjected to correlation analysis, which showed the presence of a strong cluster of variables-mainly familiarity, difficulty, and meaningfulness-when literary metaphor were presented in isolation. A weaker cluster was observed when literary metaphors were presented in the original contexts, with familiarity no longer correlating with meaningfulness. Context manipulation influenced familiarity, concreteness and difficulty ratings, which were lower in context than out of context, while meaningfulness increased. Throughout the different dimensions, the literary context seems to promote a global interpretative activity that enhances the open-endedness of the metaphor as a semantic structure constantly open to all possible interpretations intended by the author and driven by the text. This dataset will be useful for the design of future experimental studies both on literary metaphor and on the role of context in figurative meaning, combining ecological validity and aesthetic aspects of language.


Assuntos
Compreensão , Idioma , Metáfora , Psicolinguística , Adolescente , Adulto , Feminino , Humanos , Julgamento , Masculino , Adulto Jovem
2.
Front Hum Neurosci ; 8: 279, 2014.
Artigo em Inglês | MEDLINE | ID: mdl-24860470

RESUMO

According to the Perceptual Assimilation Model (PAM), articulatory similarity/dissimilarity between sounds of the second language (L2) and the native language (L1) governs L2 learnability in adulthood and predicts L2 sound perception by naïve listeners. We performed behavioral and neurophysiological experiments on two groups of university students at the first and fifth years of the English language curriculum and on a group of naïve listeners. Categorization and discrimination tests, as well as the mismatch negativity (MMN) brain response to L2 sound changes, showed that the discriminatory capabilities of the students did not significantly differ from those of the naïve subjects. In line with the PAM model, we extend the findings of previous behavioral studies showing that, at the neural level, classroom instruction in adulthood relies on assimilation of L2 vowels to L1 phoneme categories and does not trigger improvement in L2 phonetic discrimination. Implications for L2 classroom teaching practices are discussed.

3.
J Agric Food Chem ; 62(8): 1846-51, 2014 Feb 26.
Artigo em Inglês | MEDLINE | ID: mdl-24483134

RESUMO

Recently, the enzymatic hydrolysis of Lupinus albus and Lupinus angustifolius proteins with pepsin was showed to produce peptides able to inhibit the angiotensin-converting enzyme (ACE). The objective of the present work was to test different hydrolytic enzymes and to investigate three lupin species (L. albus, L. angustifolius, Lupinus luteus) with the final goal of selecting the best enzyme/species combination for an efficient production of ACE-inhibitory peptide mixtures. Pepsin gave peptides with the best IC50 values (mean value on three species 186 ± 10 µg/mL), followed by pepsin + trypsin (198 ± 16 µg/mL), chymotrypsin (213 ± 83 µg/mL), trypsin (405 ± 54 µg/mL), corolase PP (497 ± 32 µg/mL), umamizyme (865 ± 230 µg/mL), and flavourzyme (922 ± 91 µg/mL). The three species showed similar activity scales, but after pepsin + trypsin and chymotrypsin treatments, L. luteus peptide mixtures resulted to be significantly the most active. This investigation indicates that lupin proteins may be a valuable source of ACE-inhibitory peptides, which may explain the activity observed in experimental and clinical studies and foresee the application of lupin proteins into functional foods or dietary supplements.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/química , Bioquímica/métodos , Lupinus/química , Peptídeo Hidrolases/química , Peptídeos/química , Proteínas de Plantas/química , Inibidores da Enzima Conversora de Angiotensina/isolamento & purificação , Hidrólise , Peptídeos/isolamento & purificação
4.
Food Chem ; 145: 34-40, 2014 Feb 15.
Artigo em Inglês | MEDLINE | ID: mdl-24128446

RESUMO

The objective of this investigation was to compare the angiotensin converting enzyme (ACE)-inhibitory activity of the hydrolysates obtained by pepsin digestion of proteins of some legumes, such as chickpea, common bean, lentil, lupin, pea, and soybean, by using the same experimental procedure. The ACE-inhibitory activity was measured by using the tripeptide hippuryl-histidyl-leucine (HHL), as model peptide, and HPLC-DAD, as analytical method. The peptide mixtures of all legumes were active, with soybean and lupin the most efficient, with IC50 values of 224 and 226 µg/ml, respectively. Considering the promising results obtained with lupin, and aiming to identify the protein(s) that release(s) the peptides responsible for the activity, the peptides obtained from the pepsin digestion of some industrial lupin protein isolates and purified protein fractions were tested. The most active mixture, showing an IC50 value of 138 µg/ml, was obtained hydrolysing a mixture of lupin α+ß conglutin.


Assuntos
Inibidores da Enzima Conversora de Angiotensina/farmacologia , Fabaceae/química , Lupinus/química , Peptídeos/farmacologia , Hidrolisados de Proteína/farmacologia , Cromatografia Líquida de Alta Pressão/métodos
5.
Proteomics ; 9(2): 272-86, 2009 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-19105171

RESUMO

Quantitative proteomics based on MS is useful for pointing out the differences in some food proteomes relevant to human nutrition. Stable isotope label-free (SIF) techniques are suitable for comparing an unlimited number of samples by the use of relatively simple experimental workflows. We have developed an internal standard label-free method based on the intensities of peptide precursor ions from MS/MS spectra, collected in data dependent runs, for the simultaneous qualitative characterization and relative quantification of storage proteins of Lupinus albus seeds in protein extracts of four lupin cultivars (cv Adam, Arés, Lucky, Multitalia). The use of an innovative microfluidic system, the HPLC-Chip, coupled with a classical IT mass spectrometer, has allowed a complete qualitative characterization of all proteins. In particular, the homology search mode has permitted to identify single amino acid substitutions in the sequences of vicilins (beta-conglutin precursor and vicilin-like protein). The MS/MS sequencing of substituted peptides confirms the high heterogeneity of vicilins according to the peculiar characteristics of the vicilin-encoding gene family. Two suitable bioinformatics parameters were optimized for the differential analyses of the main bioactive proteins: the "normalized protein average of common reproducible peptides" (N-ACRP) for gamma-conglutin, which is a homogeneous protein, and the "normalized protein mean peptide spectral intensity" (N-MEAN) for the highly heterogenous class of the vicilins.


Assuntos
Lupinus/metabolismo , Nanotecnologia/métodos , Proteínas de Armazenamento de Sementes/análise , Sementes/química , Sequência de Aminoácidos , Substituição de Aminoácidos , Análise de Variância , Cromatografia Líquida de Alta Pressão/métodos , Biologia Computacional , Bases de Dados de Proteínas , Dados de Sequência Molecular , Peptídeos/análise , Proteínas de Vegetais Comestíveis/análise , Análise Serial de Proteínas/métodos , Padrões de Referência , Espectrometria de Massas em Tandem/métodos
6.
J Agric Food Chem ; 56(12): 4450-6, 2008 Jun 25.
Artigo em Inglês | MEDLINE | ID: mdl-18491913

RESUMO

The objective of this study was to monitor the changes in isoflavone content in different plant organs (leaves, stems, roots) during the crop growth stage of three cultivars of Lupinus albus (white lupin) under field conditions, taking into account sowing time effects (autumn and early spring) and cultivar effects. Three sampling dates (from late vegetative to late grain growth stages) were evaluated. Seven isoflavones and four flavonoids were identified by LC-ESI-MS analysis. The isoflavone content was higher in leaves than in stems, and it was highest before flowering, whereas it decreased during maturity. Autumn-sown plants showed higher isoflavone content than early spring-sown plants, especially in late vegetative and early reproductive stages. Genistein 7- O-glucoside was the main isoflavone of leaves and stems in the late vegetative stages of early spring sowing, whereas genistein was the main isoflavone under autumn sowing. Variation among cultivars affected only marginally the total isoflavone content. No isoflavones were detected in seeds.


Assuntos
Isoflavonas/análise , Lupinus/química , Lupinus/crescimento & desenvolvimento , Flavonoides/análise , Folhas de Planta/química , Raízes de Plantas , Caules de Planta/química , Estações do Ano
7.
J Agric Food Chem ; 56(10): 3657-63, 2008 May 28.
Artigo em Inglês | MEDLINE | ID: mdl-18433102

RESUMO

The intake of lupin-based foods could imply the exposure of consumers to quinolizidine alkaloids. The objectives of this study were to assess the genetic variation among and within 11 geographic regions of Lupinus albus ecotypes, verify the quinolizidine alkaloids amount of alkaloid-poor L. albus and Lupinus angustifolius varieties, and assess the effect of two climatically contrasting Italian environments on the alkaloid content. The quantitation was performed by GC-MS, and in all samples lupanine was the most abundant quinolizidine alkaloid, followed by albine and 13alpha-hydroxylupanine for L. albus and by 13alpha-hydroxylupanine and angustifoline for L. angustifolius. Some regions tended to have a high (Azores) or low (Egypt, Near East, Maghreb) total alkaloids content, but the variation among ecotypes within regions was larger than that among regions following the estimation of variance components. Alkaloid-poor varieties tended to have higher total alkaloid contents when grown in the subcontinental climate site, exceeding in some cases the limit of 0.200 mg/g.


Assuntos
Alcaloides/análise , Lupinus/genética , Quinolizidinas/análise , Sementes/química , Clima , Variação Genética , Genótipo , Itália , Lupinus/química , Especificidade da Espécie
8.
Mol Nutr Food Res ; 52(4): 490-5, 2008 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-18324702

RESUMO

Lupin proteins are gaining attention to replace animal proteins and other plants ingredients in several foods such as bakery products, imitation dairy and meat products, and beverages. One of the major safety issues of lupin-based foods is the presence of quinolizidine alkaloids (QAs), bitter compounds produced by lupin plants as a defense mechanism against predators. In mammals, QA intoxication is characterized by trembling, shaking, excitation, and convulsion. Lupanine and sparteine, the most common QAs, show acute oral toxicity due to neurological effects leading to the loss of motor co-ordination and muscular control. In this paper, 27 samples of lupin-based products, i. e., flours, protein isolates, and food (either model or commercially available ones), were analyzed for evaluating the QA content using a method based on GC/MS. All the analyzed samples were safe since they respect the maximum limit of 200 mg/kg fixed by the Health Authorities of Australia, New Zealand, Great Britain, and France, that have regulated this topic. The QA contents were particularly low in protein isolates and in foods containing these ingredients, indicating that their use is a very effective tool for keeping low the daily intake of QAs.


Assuntos
Alcaloides/análise , Farinha/análise , Análise de Alimentos , Lupinus/química , Quinolizidinas/análise , Alcaloides/toxicidade , Animais , Cromatografia Gasosa-Espectrometria de Massas , Humanos , Proteínas de Plantas/isolamento & purificação , Quinolizidinas/toxicidade , Convulsões/induzido quimicamente
9.
Mol Nutr Food Res ; 51(4): 431-6, 2007 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-17357980

RESUMO

Foods based on sweet lupin proteins are gaining attention from industry and consumers because of their possible role in the prevention of cardiovascular disease. When promoting lupin-based foods for inclusion in a daily diet, the thermal damage suffered during processing is of relevance to the bioactive and nutritional quality of the food product. N-(2-furoylmethyl)-L-lysine (furosine) quantification demonstrates that currently available sweet lupin protein isolates have a thermal damage comparable to or lower than other traditional food ingredients, and are a good source of lysine in non-dairy products. In lupin-based foods claiming to have cholesterol-lowering potential, shotgun proteomics offers itself as a fast and effective screening method for assessing the biological availability of active peptides. Such a method is readily applicable to other legume-enriched food products.


Assuntos
Suplementos Nutricionais , Análise de Alimentos , Manipulação de Alimentos , Temperatura Alta , Lupinus/química , Sequência de Aminoácidos , Anticolesterolemiantes , Lisina/análogos & derivados , Lisina/análise , Dados de Sequência Molecular , Peptídeos/análise , Peptídeos/química , Proteínas de Plantas/análise , Sementes/química
10.
J Agric Food Chem ; 54(1): 92-8, 2006 Jan 11.
Artigo em Inglês | MEDLINE | ID: mdl-16390183

RESUMO

This paper describes a pilot process for obtaining protein isolates from white lupin seed with improved water solubility and technofunctional properties as well as reduced thermal damage. After a careful optimization of the process parameters, two valuable food ingredients were prepared: lupin protein isolate type E, with a useful emulsifying capacity, and lupin protein isolate type F, with a high capability of foam formation and stabilization. The spray-drying process was particularly critical for inducing some thermal damage, but a careful selection of the conditions permitted ingredients having only marginally impaired lysine bioavailability to be obtained. The reproducibility of the protein extraction process was tested on two different lupin varieties.


Assuntos
Temperatura Alta , Lupinus/química , Proteínas de Plantas/isolamento & purificação , Sementes/química , Fenômenos Químicos , Físico-Química , Dessecação , Emulsificantes , Proteínas de Plantas/química , Controle de Qualidade
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...