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1.
Compr Rev Food Sci Food Saf ; 21(6): 4776-4811, 2022 11.
Artigo em Inglês | MEDLINE | ID: mdl-36254736

RESUMO

Historically, food fraud was a major public health concern which helped drive the development of early food regulations in many markets including the US and EU market. In the past 10 years, the integrity of food chains with respect to food fraud has again been questioned due to high profile food fraud cases. We provide an overview of the resulting numerous authoritative activities underway within different regions to counter food fraud, and we describe the guidance available to the industry to understand how to assess the vulnerability of their businesses and implement appropriate mitigation. We describe how such controls should be an extension of those already in place to manage wider aspects of food authenticity, and we provide an overview of relevant analytical tools available to food operators and authorities to protect supply chains. Practical Application: Practical Application of the provided information by the food industry in selecting resources (guidance document, analytical methods etc.).


Assuntos
Alimentos , Fraude , Indústria de Processamento de Alimentos , Indústria Alimentícia
2.
Nutr Rev ; 80(11): 2154-2177, 2022 10 10.
Artigo em Inglês | MEDLINE | ID: mdl-35713524

RESUMO

CONTEXT: Adequate iodine intake is essential throughout life. Key dietary sources are iodized salt and animal products, but dietary patterns in Europe are changing, for example toward lower salt intake and a more plant-based diet. OBJECTIVE: To review iodine intake (not status) in European populations (adults, children, and pregnant women) to identify at-risk groups and dietary sources. DATA SOURCES: PubMed, Embase, and Cochrane databases, as well as European national nutrition surveys were searched for data on had iodine intake (from dietary assessment) and sources of iodine, collected after 2006. DATA SELECTION: In total, 57 studies were included, comprising 22 national surveys and 35 sub-national studies. Iodine intake data were available from national surveys of children aged <10 years (n = 11), 11-17 years (n = 12), and adults (n = 15), but data from pregnancy were only available from sub-national studies. RESULTS: Iodine intake data are lacking-only 17 of 45 (38%) European countries had iodine-intake data from national surveys. Iodine intake reported from national surveys was below recommendations for: (1) children aged <10 years in 2 surveys (18%), (2) boys and girls aged 11-17 years in 6 (50%) and 8 (68%) surveys, respectively, and (3) adult men and women in 7 (47%) and 12 (80%) surveys, respectively. In pregnant women, intake was below recommendations except where women were taking iodine-containing supplements. Just 32% of national surveys (n = 7) included iodized salt when estimating iodine intake. Milk, dairy products, fish, and eggs were important contributors to intake in many countries, suggesting limited sources in plant-based diets. CONCLUSION: Results are limited by the challenges of dietary assessment for measuring iodine intake. Future national surveys should include iodine intake. Policy makers should consider dietary sources alongside any iodized salt policies when considering methods for improving population iodine intake. SYSTEMATIC REVIEW REGISTRATION: PROSPERO 2017 CRD42017075422.


Assuntos
Iodo , Cloreto de Sódio na Dieta , Animais , Feminino , Humanos , Leite/química , Estado Nutricional , Gravidez , Gestantes
3.
Cells ; 9(8)2020 08 07.
Artigo em Inglês | MEDLINE | ID: mdl-32784707

RESUMO

Details of the functional mechanisms of intrinsically disordered proteins (IDPs) in living cells is an area not frequently investigated. Here, we dissect the molecular mechanism of action of an IDP in cells by detailed structural analyses based on an in-cell nuclear magnetic resonance experiment. We show that the ID stress protein (IDSP) A. thaliana Early Response to Dehydration (ERD14) is capable of protecting E. coli cells under heat stress. The overexpression of ERD14 increases the viability of E. coli cells from 38.9% to 73.9% following heat stress (50 °C × 15 min). We also provide evidence that the protection is mainly achieved by protecting the proteome of the cells. In-cell NMR experiments performed in E. coli cells show that the protective activity is associated with a largely disordered structural state with conserved, short sequence motifs (K- and H-segments), which transiently sample helical conformations in vitro and engage in partner binding in vivo. Other regions of the protein, such as its S segment and its regions linking and flanking the binding motifs, remain unbound and disordered in the cell. Our data suggest that the cellular function of ERD14 is compatible with its residual structural disorder in vivo.


Assuntos
Proteínas de Arabidopsis/fisiologia , Escherichia coli/fisiologia , Resposta ao Choque Térmico , Proteínas Intrinsicamente Desordenadas/fisiologia , Arabidopsis/fisiologia , Escherichia coli/genética , Viabilidade Microbiana , Microrganismos Geneticamente Modificados/fisiologia , Chaperonas Moleculares/fisiologia , Ligação Proteica , Domínios Proteicos , Proteoma/metabolismo
4.
Front Mol Biosci ; 5: 83, 2018.
Artigo em Inglês | MEDLINE | ID: mdl-30234128

RESUMO

Protein quantification is essential in a great variety of biochemical assays, yet the inherent systematic errors associated with the concentration determination of intrinsically disordered proteins (IDPs) using classical methods are hardly appreciated. Routinely used assays for protein quantification, such as the Bradford assay or ultraviolet absorbance at 280 nm, usually seriously misestimate the concentrations of IDPs due to their distinct and variable amino acid composition. Therefore, dependable method(s) have to be worked out/adopted for this task. By comparison to elemental analysis as the gold standard, we show through the example of four globular proteins and nine IDPs that the ninhydrin assay and the commercial QubitTM Protein Assay provide reliable data on IDP quantity. However, as IDPs can show extreme variation in amino acid composition and physical features not necessarily covered by our examples, even these techniques should only be used for IDPs following standardization. The far-reaching implications of these simple observations are demonstrated through two examples: (i) circular dichroism spectrum deconvolution, and (ii) receptor-ligand affinity determination. These actual comparative examples illustrate the potential errors that can be incorporated into the biophysical parameters of IDPs, due to systematic misestimation of their concentration. This leads to inaccurate description of IDP functions.

5.
PLoS One ; 11(8): e0161970, 2016.
Artigo em Inglês | MEDLINE | ID: mdl-27564234

RESUMO

Protein chaperones are molecular machines which function both during homeostasis and stress conditions in all living organisms. Depending on their specific function, molecular chaperones are involved in a plethora of cellular processes by playing key roles in nascent protein chain folding, transport and quality control. Among stress protein families-molecules expressed during adverse conditions, infection, and diseases-chaperones are highly abundant. Their molecular functions range from stabilizing stress-susceptible molecules and membranes to assisting the refolding of stress-damaged proteins, thereby acting as protective barriers against cellular damage. Here we propose a novel technique to test and measure the capability for protective activity of known and putative chaperones in a semi-high throughput manner on a plate reader. The current state of the art does not allow the in vitro measurements of chaperone activity in a highly parallel manner with high accuracy or high reproducibility, thus we believe that the method we report will be of significant benefit in this direction. The use of this method may lead to a considerable increase in the number of experimentally verified proteins with such functions, and may also allow the dissection of their molecular mechanism for a better understanding of their function.


Assuntos
Chaperonas Moleculares/metabolismo , Análise Serial de Proteínas/métodos , Proteínas/metabolismo , Álcool Desidrogenase/química , Álcool Desidrogenase/metabolismo , Citrato (si)-Sintase/química , Citrato (si)-Sintase/metabolismo , L-Lactato Desidrogenase/química , L-Lactato Desidrogenase/metabolismo , Luciferases/química , Luciferases/metabolismo , Chaperonas Moleculares/química , Ligação Proteica , Dobramento de Proteína , Proteínas/química
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