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1.
Fungal Biol ; 116(2): 298-307, 2012 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-22289775

RESUMO

LaeA of Aspergillus nidulans is a putative methyltransferase and a component of the velvet complex; it is thought to mainly affect expression of genes required for the production of secondary metabolites. We found that although Aspergillus flavus CA14 laeA deletion mutants showed no aflatoxin production, expression of some of the early genes involved in aflatoxin formation, but not the later genes, could still be detected. The mutants grown in minimal medium supplemented with simple sugars and on some complex media exhibited altered conidial development. On potato dextrose agar (PDA) medium the deletion mutants showed reduced conidial chain elongation, increased production of conidiophores, and decreased colony hydrophobicity when compared to the parental strain. The loss of hydrophobicity and the other developmental changes in the laeA deletion mutants could affect the ability of the fungus to produce aflatoxins.


Assuntos
Aflatoxinas/metabolismo , Aspergillus flavus/química , Deleção de Genes , Regulação Fúngica da Expressão Gênica , Metiltransferases/genética , Metiltransferases/metabolismo , Esporos Fúngicos/química , Aspergillus flavus/genética , Aspergillus flavus/crescimento & desenvolvimento , Metabolismo dos Carboidratos , Meios de Cultura/química , Interações Hidrofóbicas e Hidrofílicas , Esporos Fúngicos/genética , Esporos Fúngicos/crescimento & desenvolvimento
2.
J Agric Food Chem ; 59(13): 6933-9, 2011 Jul 13.
Artigo em Inglês | MEDLINE | ID: mdl-21595494

RESUMO

Wheat ( Triticum spp.) histones H1, H2, H3, and H4 were extracted, and H1 was further purified. The effect of these histones on specific fungi that may or may not be pathogenic to wheat was determined. These fungi included Aspergillus flavus , Aspergillus fumigatus , Aspergillus niger , Fusarium oxysporum , Fusarium verticillioides , Fusarium solani , Fusarium graminearum , Penicillium digitatum , Penicillium italicum , and Greeneria uvicola . Non-germinated and germinating conidia of these fungi were bioassayed separately. The non-germinated and germinating conidia of all Fusarium species were highly susceptible to the mixture (H1-H4) as well as pure H1, with viability losses of 99-100% found to be significant (p < 0.001) at ≤10 µM or less for the histone mixture and pure H1. F. graminearum was the most sensitive to histone activity. The histones were inactive against all of the non-germinated Penicillium spp. conidia. However, they significantly reduced the viability of the germinating conidia of the Penicillium spp. conidia, with 95% loss at 2.5 µM. Non-germinated and germinating conidia viability of the Aspergillus spp. and G. uvicola were unaffected when exposed to histones up to 10 µM. Results indicate that Fusarium spp. pathogenic to wheat are susceptible to wheat histones, indicating that these proteins may be a resistance mechanism in wheat against fungal infection.


Assuntos
Fungicidas Industriais/farmacologia , Histonas/farmacologia , Triticum/química , Aspergillus/efeitos dos fármacos , Fusarium/efeitos dos fármacos , Histonas/isolamento & purificação , Penicillium/efeitos dos fármacos , Doenças das Plantas/microbiologia , Doenças das Plantas/prevenção & controle , Sementes/química , Triticum/microbiologia
3.
J Food Sci ; 76(7): S415-22, 2011 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-22417559

RESUMO

UNLABELLED: Previous research examined sanitation treatments on cut cantaloupe tissue to deliver germicidal and food safety effects. However, an apparent compromise between volatile loss and treatment/sampling efficacy appeared. Subsequently, a physiological and volatile reassessment of thinly sliced tissue against cubes was performed in cantaloupe tissue. Thin sliced cantaloupe L* decreased 27.5%, 40.5%, and 52.9% in 3, 2, and 1 mm thickness, respectively, compared with cut cubes after 3 d. Overall color (C) decreased in freshly prepared cubes (2.4%) and slices (14.4%) that were washed in cold water. Surface area per unit volume (SA: vol) in slices was 4.1 times greater than typical cubes, as reflected by substantial water loss (20.4%, 9.5%, and 6.7% in 1, 2 and 3-mm slices, respectively) after 1 d at 5 °C. Rinsing cubes and thin-slices with 5 °C deionized water resulted in roughly 15% soluble solids loss. SEM indicated 65.4% reduced cell size in 1-d old thin slices, evidenced by excessive cell damage and desiccation compared with stored fresh-cut cubes. In thin-sliced tissue exposed 15 min to an open atmosphere (mimic sanitation treatments), total esters decreased 92.8% and 95.8%, respectively, after 1 and 3 d storage at 5 °C. Washing tissue provided a boundary layer that reduced short-term ester losses in slices and cubes. Excessive cutting, sanitation treatment regimes, and storage can radically alter the desirable volatile profile of cut cantaloupe. Reduction of tissue size to maximize food-safety sanitation efficacy or delivering items to a niche market will need substantial work to engineer equipment and develop protocols to insure that product quality and volatiles are not compromised. PRACTICAL APPLICATION: We have demonstrated that cutting method and sampling protocol are critically important when using volatiles as a means by which to assess or interpret stress response and ascribe fresh-cut quality. Reduction of tissue size to maximize food-safety sanitation efficacy (for example, thin slices) will need substantial work to engineer equipment and design protocols to insure product quality and volatile profiles are not compromised.


Assuntos
Cucumis melo , Manipulação de Alimentos/métodos , Frutas/química , Frutas/ultraestrutura , Compostos Orgânicos Voláteis/análise , Cor , Cromatografia Gasosa-Espectrometria de Massas , Microscopia Eletrônica de Varredura , Controle de Qualidade , Água
4.
Langmuir ; 22(13): 5894-9, 2006 Jun 20.
Artigo em Inglês | MEDLINE | ID: mdl-16768526

RESUMO

The paper describes the effect of an oscillating magnetic field (OMF) on the morphology and release properties of collagen gels containing magnetic nanoparticles and microparticles and fluorescent drug analogues. Collagen gels were prepared through fibrillogenesis of collagen in the presence of iron oxide magnetic particles averaging 10 nm or 3 mum in diameter and rhodamine-labeled dextran (Dex-R) of molecular weights between 3000-70 000 g/mol. Dextran molecules effectively simulate protein-based drugs, since they have similar molecular weights and dimensions. The paper discusses the effect of an OMF on the release properties of the gels and proposes an empirical model to predict the release rate. It also demonstrates the self-repair capability of collagen gels following the structural damage caused by an OMF.


Assuntos
Colágeno/química , Portadores de Fármacos/química , Magnetismo , Animais , Dextranos , Sistemas de Liberação de Medicamentos , Compostos Férricos/química , Corantes Fluorescentes , Géis , Técnicas In Vitro , Nanopartículas Metálicas/química , Nanopartículas Metálicas/ultraestrutura , Microscopia Eletrônica de Varredura , Peso Molecular , Ratos , Rodaminas , Temperatura
5.
Biomaterials ; 26(34): 7164-72, 2005 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-16000221

RESUMO

The paper examines the release properties of collagen gels that contain covalently bound fluorescent drug analogs. Collagen gels were prepared by fibrilogenesis. The gels were stabilized by cross linking with EDAC/NHS. SEM studies showed that increasing the cross-linking time with EDAC/NHS resulted in decreasing pore size and increasing gel density. Fluorescence spectroscopy measurements showed a clear correlation between decreasing pore size and increasing gel density, and lower release rate from the gels. Additives like chondrotitin-6-sulfate (CS) and amino acids altered the release properties of the cross-linked collagen gels. CS increased the stability of collagen gels to enzymatic degradation and non-enzymatic degradation. This was attributed to increasing gel rigidity due to carbohydrate-protein interactions. The amino acid lysine increased the stability of collagen gels which was attributed to increasing cross-linking level between the collagen fibrils and the primary amine group on the lysine side chain. The amino acid histidine decreased the stability of the gels, particularly to non-enzymatic degradation. These results correlated with increasing pore size following treatment with histidine. Our study shows, for the first time, a clear correlation between structure and release properties of collagen gels. It describes in detail the effect of additives on the structural and release properties of collagen gels. The study focused on gels that were prepared through fibrillogenesis and were therefore similar in structure to native collagen.


Assuntos
Colágeno Tipo I/química , Portadores de Fármacos/química , Implantes de Medicamento/química , Géis/química , Preparações Farmacêuticas/administração & dosagem , Preparações Farmacêuticas/química , Espectrometria de Fluorescência/métodos , Materiais Biocompatíveis/química , Difusão , Corantes Fluorescentes , Cinética , Teste de Materiais , Conformação Molecular , Estatística como Assunto , Relação Estrutura-Atividade , Propriedades de Superfície
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