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1.
Int J Food Microbiol ; 320: 108538, 2020 May 02.
Artigo em Inglês | MEDLINE | ID: mdl-32004824

RESUMO

Neutral Electrolyzed Water (NEW) was tested in vitro and on artificially contaminated eggs against Salmonella enterica subsp. enterica or Escherichia coli. The antibacterial effect was measured 30 s after treatment. NEW microbicide activity results were compared against 2% citric acid and 0.9% saline solutions. NEW caused an in vitro decrease in Salmonella titers by ˃5.56 Log10 CFU mL-1 and in artificially contaminated eggs by ˃1.45 Log10 CFU/egg. When it was tested against E. coli, it decreased in vitro bacterial titers by ˃3.28 Log10 CFU mL-1 and on artificially contaminated eggs by ˃6.39 Log10 CFU/egg. The 2% citric acid solution caused an in vitro decrease of 0.4 Log10 CFU mL-1 of Salmonella and E. coli and on eggs artificially contaminated with E. coli or Salmonella there was a decrease of 0.06 and 0.62 Log10 CFU/egg respectively. We evaluated egg cuticle integrity by scanning electron microscopy after treatments with evaluated solutions; the 2% citric acid solution caused damage to the cuticle and exposed eggshell pores and no interaction of NEW or NaCl with the cuticle was observed. NEW treatment showed a fast-bactericidal effect in vitro and table eggs.


Assuntos
Antibacterianos/farmacologia , Casca de Ovo/microbiologia , Escherichia coli/efeitos dos fármacos , Salmonella enterica/efeitos dos fármacos , Água/farmacologia , Animais , Antibacterianos/química , Contagem de Colônia Microbiana , Casca de Ovo/efeitos dos fármacos , Ovos/microbiologia , Eletrólise , Escherichia coli/crescimento & desenvolvimento , Microbiologia de Alimentos , Concentração de Íons de Hidrogênio , Salmonella enterica/crescimento & desenvolvimento , Água/química
2.
Food Sci Nutr ; 7(7): 2252-2260, 2019 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-31367353

RESUMO

Neutral electrolyzed water (NEW) was tested as a disinfectant against Listeria monocytogenes on the surface of table eggs. Eggs were collected from a single Bovans White flock and were exposed to L. monocytogenes. Artificially contaminated eggs were divided into three different treatment groups: NEW, 2% citric acid solution (CAS), and saline solution (SS). To evaluate the bactericidal effect, the Mexican norm for antimicrobial activity determination protocol was performed. The observed bactericidal effect was compared against those obtained from CAS and SS. Bacterial cells present on the eggshells were quantified. NEW exhibited a significantly higher bactericidal effect than CAS when evaluated on the surfaces of chicken eggshells (6.11 log10CFU/ml reduction in vitro and a 2.18 log10 CFU/egg reduction on eggs vs. 1.06 log10CFU/ml in vitro reduction and 1.74 log10CFU/egg). Additionally, CAS was found to react with the carbonate egg shield, resulting in a loss of cuticle integrity. Mineral content of NEW-treated eggshells was similar to SS-treated eggshells; however, CAS-treated eggshells showed a significant decrease in phosphorous concentration compared to NEW treatment. In this study, we demonstrated the effect of NEW and CAS on the integrity of the L. monocytogenes wall using transmission electron microscopy. To the best of our knowledge, this is the first report of the effect of NEW against L. monocytogenes on eggshells. Our results show that NEW is a viable alternative solution for the disinfection of table eggs that does not affect the cuticle or shell.

3.
Histochem Cell Biol ; 150(5): 521-527, 2018 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-30206694

RESUMO

Light and electron microscopy have been used to study cell structure for many years, but atomic force microscopy is a more recent technique used to analyze cells, mainly due to the absence of techniques to prepare the samples. Isolated molecules or organelles, whole cells, and to a lesser extent in situ cell structure have been observed by different atomic force microscopy imaging modes. Here, we review efforts intended to analyze in situ the cell structures using approaches involving imaging of the surface of semithin sections of samples embedded in resin and sections prepared with an ultramicrotome. The results of such studies are discussed in relation to their implications to analyze the fine structure of organelles at the nanoscale in situ at enhanced resolution compared to light microscopy.


Assuntos
Linfócitos/citologia , Linfócitos/ultraestrutura , Microscopia de Força Atômica , Organelas/ultraestrutura , Animais , Resinas Epóxi/química , Humanos , Linfócitos/química , Organelas/química
4.
Mol Biol Cell ; 23(6): 1115-28, 2012 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-22262462

RESUMO

The mammalian cell nucleus is functionally compartmentalized into various substructures. Nuclear speckles, also known as interchromatin granule clusters, are enriched with SR splicing factors and are implicated in gene expression. Here we report that nuclear speckle formation is developmentally regulated; in certain cases phosphorylated SR proteins are absent from the nucleus and are instead localized at granular structures in the cytoplasm. To investigate how the nuclear architecture is formed, we performed a phenotypic screen of HeLa cells treated with a series of small interfering RNAs. Depletion of Ran-binding protein 2 induced cytoplasmic intermediates of nuclear speckles in G1 phase. Detailed analyses of these structures suggested that a late step in the sequential nuclear entry of mitotic interchromatin granule components was disrupted and that phosphorylated SR proteins were sequestered in an SR protein kinase-dependent manner. As a result, the cells had an imbalanced subcellular distribution of phosphorylated and hypophosphorylated SR proteins, which affected alternative splicing patterns. This study demonstrates that the speckled distribution of phosphorylated pre-mRNA processing factors is regulated by the nucleocytoplasmic transport system in mammalian cells and that it is important for alternative splicing.


Assuntos
Processamento Alternativo , Núcleo Celular/química , Núcleo Celular/metabolismo , Chaperonas Moleculares/metabolismo , Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo , Proteínas Nucleares/metabolismo , Proteínas de Ligação a RNA/metabolismo , Animais , Grânulos Citoplasmáticos/metabolismo , Fase G1 , Humanos , Camundongos , Proteínas Nucleares/análise , Proteínas de Transporte Nucleocitoplasmático/metabolismo , Fosforilação , Proteínas de Ligação a RNA/análise , Fatores de Processamento de Serina-Arginina
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