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1.
J Funct Foods ; 48: 410-419, 2018 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-30344649

RESUMO

The aim was to incorporate vegetables containing the phytochemicals quercetin, apigenin, glucoraphanin and carotenoids into a processed potato-based snack and assess their bioaccessibility and bioavailability. Three different processing routes were tested for incorporation and retention of phytochemicals in snacks using individually quick frozen or freeze-dried vegetables. No significant differences in the uptake or transport of quercetin or apigenin between a vegetable mix or snacks were observed using the CaCo-2 transwell model. Simulated in vitro digestions predicted a substantial release of quercetin and apigenin, some release of glucoraphanin but none for carotenes from either the snack or equivalent steamed vegetables. In humans, there were no significant differences in the bioavailability of quercetin, apigenin or glucoraphanin from the snack or equivalent steamed vegetables. We have shown that significant quantities of freeze-dried vegetables can be incorporated into snacks with good retention of phytochemicals and with similar bioavailability to equivalent steamed vegetables.

2.
J Bacteriol ; 194(15): 3814-23, 2012 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-22609917

RESUMO

The food-borne bacterial pathogen Campylobacter jejuni efficiently utilizes organic acids such as lactate and formate for energy production. Formate is rapidly metabolized via the activity of the multisubunit formate dehydrogenase (FDH) enzyme, of which the FdhA subunit is predicted to contain a selenocysteine (SeC) amino acid. In this study we investigated the function of the cj1500 and cj1501 genes of C. jejuni, demonstrate that they are involved in selenium-controlled production of FDH, and propose the names fdhT and fdhU, respectively. Insertional inactivation of fdhT or fdhU in C. jejuni resulted in the absence of FdhA and FdhB protein expression, reduced fdhABC RNA levels, the absence of FDH enzyme activity, and the lack of formate utilization, as assessed by (1)H nuclear magnetic resonance. The fdhABC genes are transcribed from a single promoter located two genes upstream of fdhA, and the decrease in fdhABC RNA levels in the fdhU mutant is mediated at the posttranscriptional level. FDH activity and the ability to utilize formate were restored by genetic complementation with fdhU and by supplementation of the growth media with selenium dioxide. Disruption of SeC synthesis by inactivation of the selA and selB genes also resulted in the absence of FDH activity, which could not be restored by selenium supplementation. Comparative genomic analysis suggests a link between the presence of selA and fdhTU orthologs and the predicted presence of SeC in FdhA. The fdhTU genes encode accessory proteins required for FDH expression and activity in C. jejuni, possibly by contributing to acquisition or utilization of selenium.


Assuntos
Campylobacter jejuni/enzimologia , Campylobacter jejuni/metabolismo , Formiato Desidrogenases/metabolismo , Regulação Bacteriana da Expressão Gênica , Selênio/metabolismo , Formiatos/metabolismo , Deleção de Genes , Perfilação da Expressão Gênica , Teste de Complementação Genética , Espectroscopia de Ressonância Magnética , Mutagênese Insercional , Regiões Promotoras Genéticas , Transcrição Gênica
3.
Am J Clin Nutr ; 91(4): 923-31, 2010 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-20181815

RESUMO

BACKGROUND: Dietary recommendations for selenium differ between countries, mainly because of uncertainties over the definition of optimal selenium status. OBJECTIVE: The objective was to examine the dose-response relations for different forms of selenium. DESIGN: A randomized, double-blind, placebo-controlled dietary intervention was carried out in 119 healthy men and women aged 50-64 y living in the United Kingdom. Daily placebo or selenium-enriched yeast tablets containing 50, 100, or 200 microg Se ( approximately 60% selenomethionine), selenium-enriched onion meals ( approximately 66% gamma-glutamyl-methylselenocysteine, providing the equivalent of 50 microg Se/d), or unenriched onion meals were consumed for 12 wk. Changes in platelet glutathione peroxidase activity and in plasma selenium and selenoprotein P concentrations were measured. RESULTS: The mean baseline plasma selenium concentration for all subjects was 95.7 +/- 11.5 ng/mL, which increased significantly by 10 wk to steady state concentrations of 118.3 +/- 13.1, 152.0 +/- 24.3, and 177.4 +/- 26.3 ng/mL in those who consumed 50, 100, or 200 microg Se-yeast/d, respectively. Platelet glutathione peroxidase activity did not change significantly in response to either dose or form of selenium. Selenoprotein P increased significantly in all selenium intervention groups from an overall baseline mean of 4.99 +/- 0.80 microg/mL to 6.17 +/- 0.85, 6.73 +/- 1.01, 6.59 +/- 0.64, and 5.72 +/- 0.75 microg/mL in those who consumed 50, 100, or 200 microg Se-yeast/d and 50 microg Se-enriched onions/d, respectively. CONCLUSIONS: Plasma selenoprotein P is a useful biomarker of status in populations with relatively low selenium intakes because it responds to different dietary forms of selenium. To optimize the plasma selenoprotein P concentration in this study, 50 microg Se/d was required in addition to the habitual intake of approximately 55 microg/d. In the context of established relations between plasma selenium and risk of cancer and mortality, and recognizing the important functions of selenoprotein P, these results provide important evidence for deriving estimated average requirements for selenium in adults. This trial was registered at clinicaltrials.gov as NCT00279812.


Assuntos
Glutationa Peroxidase/sangue , Estado Nutricional , Selênio/administração & dosagem , Selênio/sangue , Selenoproteína P/sangue , Oligoelementos/administração & dosagem , Biomarcadores/sangue , Plaquetas/efeitos dos fármacos , Dieta , Suplementos Nutricionais , Método Duplo-Cego , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Necessidades Nutricionais , Cebolas , Oligoelementos/sangue , Reino Unido , Leveduras
4.
Am J Clin Nutr ; 85(6): 1557-64, 2007 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-17556693

RESUMO

BACKGROUND: Discrepancies have been reported between estimates of the prevalence of riboflavin deficiency based on intakes of riboflavin and estimates based on measures of riboflavin status. One reason for this may be an overestimate of the bioavailability of riboflavin from foods, about which relatively little is known. OBJECTIVE: We aimed to quantify the bioavailability of riboflavin from milk and spinach by using stable-isotope labels and a urinary monitoring technique and by a plasma appearance method based on kinetic modeling. DESIGN: Twenty healthy women aged 18-65 y were recruited for a randomized crossover study performed with extrinsically labeled (13C) milk and intrinsically labeled (15N) spinach as sources of riboflavin. An intravenous bolus of labeled riboflavin was administered with each test meal to assess the apparent volume of distribution of riboflavin in plasma. RESULTS: No significant differences were noted in riboflavin absorption from the spinach meal and from the milk meal according to either the urinary monitoring technique (60 +/- 8.0% and 67 +/- 5.4%, respectively; P = 0.549) or the plasma appearance method (20 +/- 2.8% and 23 +/- 5.3%, respectively; P = 0.670). CONCLUSIONS: A large fraction of newly absorbed riboflavin is removed by the liver on "first pass." The plasma appearance method therefore underestimates riboflavin bioavailability and should not be used to estimate riboflavin bioavailability from foodstuffs. Urinary monitoring suggests that riboflavin from spinach is as bioavailable as is riboflavin from milk.


Assuntos
Leite , Riboflavina/farmacocinética , Spinacia oleracea , Adsorção , Adulto , Animais , Disponibilidade Biológica , Estudos Cross-Over , Feminino , Flavinas/sangue , Flavinas/urina , Alimentos , Humanos , Marcação por Isótopo , Cinética , Pessoa de Meia-Idade , Leite/química , Riboflavina/análise , Riboflavina/sangue , Spinacia oleracea/química
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