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1.
Sensors (Basel) ; 23(6)2023 Mar 07.
Artigo em Inglês | MEDLINE | ID: mdl-36991609

RESUMO

LIDAR is an atmospheric sounding instrument based on the use of high-power lasers. The use of these lasers involves fulfilling obligations with respect to air safety. In this article, we present a low-cost air traffic surveillance solution integrated into an automated operating system for the Rayleigh-Mie-Raman LIDAR of Clermont Ferrand and the statistical elements of its application over more than two years of operation from September 2019 to March 2022. Air traffic surveillance that includes the possibility of shutting off lasers is required by international regulations because LIDAR is equipped with a class four laser that presents potential dangers to aircraft flying overhead. The original system presented in this article is based on software-defined radio. ADS-B transponder frames are analyzed in real-time, and laser emission is stopped during LIDAR operation when an aircraft is detected within a 2 km radius around the LIDAR. The system was accredited in 2019 by the French air traffic authorities. Laser shutdowns due to the detection of aircraft near the Clermont Ferrand LIDAR caused a data loss rate of less than 2% during the period of application.

2.
J Agric Food Chem ; 64(3): 699-705, 2016 Jan 27.
Artigo em Inglês | MEDLINE | ID: mdl-26727622

RESUMO

To better understand the relationship between the muscle structure and NaCl transfers in meat, we used energy-dispersive X-ray spectroscopy (EDS) coupled with scanning electron microscopy (SEM) to analyze brined and dry-salted rat muscles. The muscles were freeze-dried to avoid the delocalization of soluble ions that happens in regular dehydration through a graded series of ethanol. Na and Cl maps were superimposed on SEM images to combine the muscle structure and NaCl diffusion. Brining causes rapid diffusion of NaCl through the tissue. Most brine diffuses in a linear front from the muscle surface, but a small proportion enters through the perimysium network. The muscle area penetrated by brine shows heterogeneous patterns of NaCl retention, with some connective tissue islets containing more NaCl than other parts of perimysium. NaCl penetration is considerably slower after dry salting than after brining.


Assuntos
Músculo Esquelético/química , Cloreto de Sódio/química , Animais , Difusão , Carne/análise , Músculo Esquelético/metabolismo , Ratos , Sais/química , Cloreto de Sódio/metabolismo , Espectrometria por Raios X
3.
Analyst ; 140(12): 4189-96, 2015 Jun 21.
Artigo em Inglês | MEDLINE | ID: mdl-25912941

RESUMO

The rat skeletal muscle consists of four pure types of muscle cells called type I, type IIA, type IIX and type IIB, and their hybrids in different proportions. They differ in their contraction speeds and metabolic pathways. The intracellular composition is adapted to the fibre function and therefore to fibre types. Given that small differences in composition are likely to alter the optical properties of the cells, we studied the impact of the cell type on the fluorescence response following excitation in the deep UV region. Rat soleus and extensor digitorum longus (EDL) muscle fibres, previously identified based on their cell types by immunohistofluorescence analysis, were analyzed by synchrotron fluorescence microspectroscopy on stain-free serial muscle cross-sections. Muscle fibres excited at 275 nm showed differences in the fluorescence emission intensity among fibre types at 302, 325, 346 and 410 nm. The 410/325 ratio decreased significantly with contractile and metabolic features in EDL muscle, in the order of I > IIA > IIX > IIB fibres (p < 0.01). Compared to type I fibres, the 346/302 ratio of IIA fibres decreased significantly in both EDL and soleus muscles (p < 0.01). This study highlights the usefulness of autofluorescence spectral signals to characterize histological cross-sections of muscle fibres with no staining chemicals.


Assuntos
Fibras Musculares Esqueléticas/química , Fibras Musculares Esqueléticas/efeitos da radiação , Raios Ultravioleta , Animais , Masculino , Ratos , Ratos Wistar , Espectrometria de Fluorescência
4.
J Agric Food Chem ; 62(25): 5954-62, 2014 Jun 25.
Artigo em Inglês | MEDLINE | ID: mdl-24856923

RESUMO

Denaturation of the protein matrix during heat treatment of duck foie gras was studied in relationship to the amount of fat loss during cooking. A low fat loss group was compared with a high fat loss group by histochemistry, FT-IR, and synchrotron UV microspectroscopy combination to characterize their protein matrix at different scales. After cooking, the high fat loss group showed higher densification of its matrix, higher ultraviolet tyrosine autofluorescence, and an infrared shift of the amide I band. These results revealed a higher level of protein denaturation and aggregation during cooking in high fat loss than in low fat loss foie gras. In addition, the fluorescence and infrared responses of the raw tissue revealed differences according to the level of fat losses after cooking. These findings highlight the importance of the supramolecular state of the protein matrix in determining the fat loss of foie gras.


Assuntos
Gorduras/química , Fígado/química , Proteínas/química , Animais , Culinária , Patos , Temperatura Alta , Espectrofotometria Ultravioleta
5.
PLoS One ; 8(3): e59386, 2013.
Artigo em Inglês | MEDLINE | ID: mdl-23516631

RESUMO

Enterohemorrhagic Escherichia coli (EHEC) O157:H7 are responsible for repeated food-poisoning cases often caused by contaminated burgers. EHEC infection is predominantly a pediatric illness, which can lead to life-threatening diseases. Ruminants are the main natural reservoir for EHEC and food contamination almost always originates from faecal contamination. In beef meat products, primary bacterial contamination occurs at the dehiding stage of slaughtering. The extracellular matrix (ECM) is the most exposed part of the skeletal muscles in beef carcasses. Investigating the adhesion to the main muscle fibrous ECM proteins, insoluble fibronectin, collagen I, III and IV, laminin-α2 and elastin, results demonstrated that the preceding growth conditions had a great influence on subsequent bacterial attachment. In the tested experimental conditions, maximal adhesion to fibril-forming collagens I or III occurred at 25°C and pH 7. Once initially adhered, exposure to lower temperatures, as applied to meat during cutting and storage, or acidification, as in the course of post-mortem physiological modifications of muscle, had no effect on detachment, except at pHu. In addition, dense biofilm formation occurred on immobilized collagen I or III and was induced in growth medium supplemented with collagen I in solution. From this first comprehensive investigation of EHEC adhesion to ECM proteins with respect to muscle biology and meat processing, new research directions for the development of innovative practices to minimize the risk of meat contamination are further discussed.


Assuntos
Colágeno Tipo III/farmacologia , Colágeno Tipo I/farmacologia , Matriz Extracelular/metabolismo , Animais , Biofilmes/efeitos dos fármacos , Bovinos , Meios de Cultura/farmacologia , Elastina/metabolismo , Escherichia coli/metabolismo , Fibronectinas/metabolismo , Concentração de Íons de Hidrogênio , Laminina/metabolismo , Temperatura
6.
Food Chem ; 134(2): 1044-51, 2012 Sep 15.
Artigo em Inglês | MEDLINE | ID: mdl-23107726

RESUMO

The thermal denaturation of proteins in skeletal muscle was studied and characterised for the first time taking into account the in situ metabolic and contractile fibre types. From serial histological sections, collagen, elastin, various type I, IIa and IIx fibres and type I-IIa and IIa-IIx hybrids were identified by immunohistofluorescence. Histological sections were incubated in buffer solutions at increasing temperatures (40, 50, 60, 70 and 80°C). Protein secondary structure was investigated by synchrotron radiation FT-IR microspectroscopy on connective tissue and in muscle fibres rigorously identified for sub-type. Whatever the target protein components, increasing temperature resulted in a decrease in α-helix secondary structure and an increase in ß-sheet structure. This phenomenon was more pronounced for intracellular proteins than for connective tissue. Although hybrid fibres were generally somewhat less sensitive to unfolding than the pure types, the amplitude of the thermal denaturation of intracellular proteins was practically independent of fibre type.


Assuntos
Imuno-Histoquímica/métodos , Proteínas Musculares/química , Miofibrilas/química , Espectroscopia de Infravermelho com Transformada de Fourier/métodos , Animais , Bovinos , Desnaturação Proteica , Estrutura Secundária de Proteína , Espectroscopia de Infravermelho com Transformada de Fourier/instrumentação , Temperatura
7.
Food Chem ; 132(3): 1387-1394, 2012 Jun 01.
Artigo em Inglês | MEDLINE | ID: mdl-29243627

RESUMO

Histochemical and structural characteristics were investigated in Gastrocnemius pars interna (GN) and Iliofiburalis (IF) limb muscles of Rhea americana. The average myofibre area cross-section was greater in GN than IF muscle (p<0.001), whereas the fibre density per section was higher in IF than GN muscle. The only type of myofibre found in both the rhea limb muscles analysed in this study was fast-twitch oxidative-glycolytic fibres (FOG). Immunolabelling analysis and ultrastructural observation of myofibres confirmed the contractile and metabolic characteristics of rhea myofibres, revealing the absolute fast isoform of myosin heavy chain and the abundance of glycogen and mitochondria inside the cells, mainly in IF muscle. These findings converged with previous results on the biochemical and physicochemical characteristics of rhea meat to provide further evidence that myofibre composition substantially influences the oxidative reactions of the muscle and therefore the meat quality, but more in-depth examination is needed to establish the links between myofibre characteristics, myofibre glycogen concentration and meat stability during storage.

8.
Meat Sci ; 88(1): 28-35, 2011 May.
Artigo em Inglês | MEDLINE | ID: mdl-21183286

RESUMO

Among the techniques based on light interactions with biological tissues, fluorescence polarization offers a selective means of characterizing the organization of biological tissues. This paper presents a methodology for investigating the fluorescence polarization of muscle tissues in to obtain structural information, and specifically the structural modifications caused by meat ageing. A theoretical model of fluorescence anisotropy based on geometrical distribution and properties of tryptophan, the major fluorophore in muscle tissues, is proposed. Experimental data are fitted with the model and fitting parameters (C(1), C(2) and τ) are tracked during meat ageing. Results presented demonstrate how the method is able to show muscle structure modification during ageing. They highlight changes in structural proteins along the main axis of myofibrils and changes in the tryptophan environment resulting from the physicochemical and enzymatic processes at work during ageing.


Assuntos
Polarização de Fluorescência/métodos , Carne/análise , Proteínas Musculares/química , Animais , Anisotropia , Bovinos , Corantes Fluorescentes/química , Miofibrilas/metabolismo , Fatores de Tempo , Triptofano/química
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