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1.
J Agric Food Chem ; 56(4): 1289-97, 2008 Feb 27.
Artículo en Inglés | MEDLINE | ID: mdl-18211016

RESUMEN

The aim of this research was to study uracil and lactic and acetic acids as chemical markers for hygienic quality evaluation of raw material in liquid pasteurized egg products. Uracil, absent in sound whole eggs, was formed in raw and pasteurized egg products as a consequence of high microbial contamination (>10(6) cfu/g) after a sufficient lag time, remaining stable at 4 degrees C but disappearing after 7 days of storage at 25 degrees C. Both lactic and acetic acids, starting from initial values of 1-7 mg/kg dry matter, presented trends similar to that of uracil; however, acetic acid never decreased during the storage of raw egg products. With few exceptions, all three metabolites were produced by Enterobacter cloacae, Escherichia coli, Morganella morganii, Serratia liquefaciens, Aeromonas hydrophyla, Pseudomonas fluorescens, Enterococcus avium, and Enterococcus faecalis, separately inoculated in whole egg samples. Uracil seems to be the most sensible marker, with a suggested limit corresponding to the detectable level.


Asunto(s)
Huevos , Contaminación de Alimentos/análisis , Microbiología de Alimentos , Higiene , Ácido Acético/análisis , Animales , Recuento de Colonia Microbiana , Huevos/análisis , Huevos/microbiología , Huevos/normas , Humanos , Ácido Láctico/análisis , Temperatura , Factores de Tiempo , Uracilo/análisis
2.
J Agric Food Chem ; 53(2): 349-55, 2005 Jan 26.
Artículo en Inglés | MEDLINE | ID: mdl-15656671

RESUMEN

The aim of this research was to evaluate the suitability of uracil as an hygienic quality index of tomato products. Whereas uridine was naturally present throughout tomato fruits' ripening, uracil appeared only after microbial contamination. In tomato pulp inoculated with nine different microbial strains, all five lactic acid bacteria (LAB) studied released relevant quantities of uracil (150-1040 mg/kg of dm), with a correlated partial or total decrease of uridine. Uracil production by yeasts and molds was very low or nonexistent; the starting uridine concentration (approximately 960 mg/kg of dm) remained constant or increased. Uracil thermostability was also verified. Twenty-six samples of tomato paste (30 degrees Brix) were collected from bag-in-drums produced in an industrial processing plant, some with evident swelling symptoms. All of the samples with high microbial count presented uracil. Uracil was also present in samples with microbial contamination under the detection limit and Howard mold count below legislation limits, implying the reprocessing, at least partial, of altered tomato product. The results indicate that uracil presence in tomato products is an index of LAB contamination that has occurred before heat treatment.


Asunto(s)
Microbiología de Alimentos , Lactobacillus , Leuconostoc , Pediococcus , Solanum lycopersicum/microbiología , Uracilo/análisis , Estabilidad de Medicamentos , Calor , Uridina/análisis
3.
Rev Sci Instrum ; 86(9): 093101, 2015 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-26429423

RESUMEN

The SPectral IMager (SPIM) facility is a laboratory visible infrared spectrometer developed to support space borne observations of rocky bodies of the solar system. Currently, this laboratory setup is used to support the DAWN mission, which is in its journey towards the asteroid 1-Ceres, and to support the 2018 Exo-Mars mission in the spectral investigation of the Martian subsurface. The main part of this setup is an imaging spectrometer that is a spare of the DAWN visible infrared spectrometer. The spectrometer has been assembled and calibrated at Selex ES and then installed in the facility developed at the INAF-IAPS laboratory in Rome. The goal of SPIM is to collect data to build spectral libraries for the interpretation of the space borne and in situ hyperspectral measurements of planetary materials. Given its very high spatial resolution combined with the imaging capability, this instrument can also help in the detailed study of minerals and rocks. In this paper, the instrument setup is first described, and then a series of test measurements, aimed to the characterization of the main subsystems, are reported. In particular, laboratory tests have been performed concerning (i) the radiation sources, (ii) the reference targets, and (iii) linearity of detector response; the instrumental imaging artifacts have also been investigated.

4.
J Agric Food Chem ; 52(26): 7997-8000, 2004 Dec 29.
Artículo en Inglés | MEDLINE | ID: mdl-15612787

RESUMEN

It has been reported that various cultivars of fruits and vegetables may present a different pattern for the contained allergens. Here, we report on the different content in allergenic proteins for different peach (Prunus persica) cultivars, sampled during two consecutive harvest seasons. Fruits from six cultivars of peaches were harvested fully ripe, and the proteins extracted from whole or chemically peeled fruits were analyzed by SDS-PAGE and immunoblotting. All the protein extracts from whole fruit contained a 9 kDa protein. This protein proved to be absent in the extracts taken from chemically peeled fruit. In four cultivars, this protein corresponds to the allergen Pru p3, a lipid transfer protein that causes the oral allergy syndrome (OAS) in sensitized people. In the following year, fruits from four of the six cultivars of peaches studied previously were harvested at different times, at one and two weeks before the commercial ripening time and when fully ripe, to ascertain whether the presence of the 9 kDa allergen might be related to the ripening process. Two cultivars out of four produced an intense allergenic band corresponding to a 9 kDa protein already two weeks before the commercial ripening date, while the others showed a progressive increment of the 9 kDa allergen during ripening.


Asunto(s)
Alérgenos/análisis , Frutas/crecimiento & desarrollo , Frutas/inmunología , Proteínas de Plantas/inmunología , Prunus/inmunología , Electroforesis en Gel de Poliacrilamida , Immunoblotting , Estaciones del Año
5.
J Agric Food Chem ; 57(22): 10749-54, 2009 Nov 25.
Artículo en Inglés | MEDLINE | ID: mdl-19919119

RESUMEN

There is an increasing consumption of tomatoes worldwide: fresh in salads, cooked in household sauces, or industrially processed. Although many tomato allergens have been identified, there is no information in the literature on the allergenic components found in commercial tomato products. The primary aim of the study was to evaluate the allergenic profile of commercial tomato products by skin prick tests (SPTs) and IgE/immunoblotting in tomato-allergic subjects. The secondary end point was the study of the IgE-binding profile of tomato peel, pulp, and seeds. Forty tomato-allergic patients, reporting oral allergy syndrome (OAS) at different grades of severity for fresh and, in some cases, also for cooked tomato, were selected on the basis of positive tomato allergy history or open food challenge (OFC). They were evaluated by SPTs with different experimental tomato extracts. SDS-PAGE/immunoblotting was performed to detect tomato allergens, which were then identified by Edman degradation. Twenty-three patients (57.5%) presented first-grade OAS at the OFC, whereas 17 (42.5%) reported severe symptoms. Ten of these 17 patients (25%) reported allergic reactions to cooked tomatoes; in immunoblotting tests, their sera reacted only to lipid transfer protein (LTP). In commercial products, LTP was the only detectable allergen. In contrast to other LTP-containing fruits, in tomato, an IgE-binding LTP was identified not only in the peel but also in the pulp and seeds. This study demonstrates that, in fresh tomato, different LTP isoforms are present and allergenic. Industrial tomato derivatives still contain LTP, thus presenting a problem for LTP-allergic patients.


Asunto(s)
Antígenos de Plantas/análisis , Antígenos de Plantas/inmunología , Proteínas Portadoras/análisis , Proteínas Portadoras/inmunología , Hipersensibilidad a los Alimentos/inmunología , Frutas/inmunología , Inmunoglobulina E/metabolismo , Proteínas de Plantas/análisis , Proteínas de Plantas/inmunología , Solanum lycopersicum/inmunología , Adulto , Femenino , Frutas/química , Humanos , Immunoblotting , Masculino , Extractos Vegetales/inmunología , Semillas/química , Semillas/inmunología , Pruebas Cutáneas
6.
J Agric Food Chem ; 56(16): 7091-9, 2008 Aug 27.
Artículo en Inglés | MEDLINE | ID: mdl-18620412

RESUMEN

The effects of an innovative process for the manufacture of peach and nectarine purees on the main quality indices, namely, color, consistency, carotenoid and phenolic content, and antioxidant activity, were studied using a peach cultivar that is optimal for nectar processing (cv. Redhaven) and peach and nectarine varieties that undergo a faster browning degradation. The innovative process, operating the pulping/finishing step at room temperature, was compared to the traditional process of hot pulping/finishing. The study comprised initial trials on a pilot plant scale and scaling up to industrial production of the puree and nectar. The quality of products was analyzed at the time of production and as a function of storage of both the puree and the nectar. With respect to the traditional process, the new process, scaled up to industrial levels, improved the color of peach and nectarine products (by increasing the L* value and decreasing the a* value), whatever the variety studied; maintained almost the same levels of carotenoids, hydroxycinnamates, flavan-3-ols, and flavonols; and reduced the level of cyanidin 3-O-glucoside. The presence of cyanidin 3-O-glucoside was correlated to an unstable and undesirable red hue of the products (even if its concentration was very low in all products), and the decreased level obtained by the innovative process was considered to be positive. On the basis of these results, new technology can be proposed for the processing of fruit varieties that are not suitable for puree production using traditional technology. This opens up two possibilities: (a) utilization of fresh market fruit surplus and (b) processing of selected fruit varieties that are rich in antioxidants but have a high browning potential, such as the Stark Red Gold nectarine. Furthermore, as the positive impact of the new technology is optimal at the beginning of storage, it is particularly suitable for fruit-based products with a short shelf life.


Asunto(s)
Antioxidantes/análisis , Color , Manipulación de Alimentos/métodos , Frutas/química , Prunus/química , Bebidas/análisis , Carotenoides/análisis , Conservación de Alimentos , Fenoles/análisis , Control de Calidad , Factores de Tiempo
7.
J Allergy Clin Immunol ; 112(4): 775-83, 2003 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-14564361

RESUMEN

BACKGROUND: In a previous study a 9-kd lipid-transfer protein (LTP) was identified as the major allergen of raw maize in a population of 22 anaphylactic patients. However, the stability of this protein in cooked maize is unknown. OBJECTIVE: We investigated the allergenicity of 5 maize hybrids and its modification after different thermal treatments by using sera from anaphylactic patients and patients with positive double-blind, placebo-controlled food challenges. METHODS: Five maize hybrids were extracted by using different methods, obtaining the water-soluble, zein, total zein, glutelin, and total protein fractions. The IgE-binding capacity of the different extracts, both raw and after thermal treatment, was investigated by means of SDS-PAGE immunoblotting. A 9-kd heat-stable allergen was purified by means of HPLC and sequenced. Changes in its secondary structure during and after heating from 25 degrees C to 100 degrees C were monitored by means of circular dichroism. RESULTS: All raw maize hybrids showed similar protein and IgE-binding profiles. The SDS-PAGE of all the heat-treated hybrids demonstrated a decreased number of stained bands in respect to the raw samples. The IgE immunoblotting demonstrated that the major allergen of the water-soluble, total zein, total protein, and glutelin fractions was a 9-kd protein identified by means of amino acid sequence as an LTP and a sub-tilisin-chymotrypsin inhibitor (in total zein fraction). The IgE-binding capacity of this 9-kd protein remained unchanged after thermal treatments, even though circular dichroism demonstrated an altered secondary structure. CONCLUSIONS: Maize LTP maintains its IgE-binding capacity after heat treatment, thus being the most eligible candidate for a causative role in severe anaphylactic reactions to both raw and cooked maize.


Asunto(s)
Alérgenos/inmunología , Anafilaxia/inmunología , Proteínas Portadoras/inmunología , Culinaria , Hipersensibilidad a los Alimentos/inmunología , Inmunoglobulina E/inmunología , Zea mays/inmunología , Adulto , Secuencia de Aminoácidos/genética , Antígenos de Plantas , Proteínas Portadoras/química , Proteínas Portadoras/genética , Método Doble Ciego , Electroforesis en Gel de Poliacrilamida , Femenino , Humanos , Immunoblotting , Masculino , Espectrometría de Masas , Persona de Mediana Edad , Proteínas de Plantas , Conformación Proteica , Temperatura
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