1,524 research outputs found

    Stability of tryptophan during food processing and storage: 2. A comparison of methods used for the measurement of tryptophan losses in processed foods

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    1. Tryptophan losses in stored milk powders and in different model systems representing the major reactions of food proteins during processing and storage were determined using four different chemical methods and in a rat assay. 2. Similar tryptophan values were obtained by the three chemical methods which included high pressure liquid chromatography (HPLC) after sodium hydroxide hydrolysis. colorimetric reaction with p-dimethylamino- benzaldehyde (p-DAB) after barium hydroxide hydrolysis, and fluorescence of the Norharman derivative after NaOH hydrolysis. 3. Tryptophan losses in the treated proteins as measured by the alkaline-hydrolysis methods were generally smaller than those determined by the rat assay. Good agreement however was obtained when the chemical value was multiplied by the true nitrogen digestibility. 4. Determination of tryptophan by reaction with p-DAB after papain (EC 3.4.22.2) digestion gave lower values in the processed proteins than the other chemical methods or the rat assay. 5. A method using alkaline-hydrolysis is recommended, preferably combined with HPLC-measurement of the liberated tryptopha

    Reactions of proteins with oxidizing lipids: 1. Analytical measurements of lipid oxidation and of amino acid losses in a whey protein-methyl linolenate model system

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    1. The reactions between protein-bound amino acids and oxidizing lipid were investigated in a whey protein-methyl linolenate (C18.3)-water model system. The extent of fat oxidation was followed by measuring oxygen uptake, hydroperoxide formation and hydrocarbon (ethane and pentane) formation. 2. Significant losses occurred with lysine (up to 71 %), tryptophan (up to 31 %) and histidine (up to 57%). Methionine was extensively oxidized to its sulphoxide but less than 2% was further oxidized to the sulphone. No other amino acids were affected. 3. Increasing storage temperature (20°, 37°, 55°) resulted in an enhancement of fat oxidation reactions and amino acid degradation. 4. Increasing water activity (0.28, 0.65, 0.90) increased losses of lysine and tryptophan but had no influence on the oxidation of methionine, the level of remaining hydroperoxides or 02 uptake. Hydrocarbons were decreased. 5. Limitation of 02 uptake to 1 mol/mol lipid instead of excess 02 (02 uptake about 2.5 mol/mol lipid in 4 weeks) significantly reduced the degradation of lysine and tryptophan but had less influence on the oxidation of methionine. The level of remaining hydroperoxides was increased but hydrocarbons were unaffecte

    Reactions of proteins with oxidizing lipids: 2. Influence on protein quality and on the bioavailability of lysine, methionine, cyst(e)ine and tryptophan as measured in rat assays

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    1. The consequences of reactions between protein and oxidizing lipids on the nutritional quality of food proteins have been investigated using a whey protein-methyl linolenate-water model system. 2. In rat assays, significant reductions were observed in protein efficiency ratio, net protein ratio, net protein utilization, biological value and true nitrogen digestibility, especially when the reaction had taken place at high moisture content, high temperature and in the presence of excess oxygen. 3. The losses of bioavailable lysine and tryptophan as measured by rat assays followed a similar pattern. The chemical value of each amino acid multiplied by the true N digestibility closely resembled the rat assay value. In general, the reaction products of lysine and tryptophan formed during lipid oxidation were biologically unavailable. 4. The bioavailabilities of methionine and of ‘methionine plus cyst(e)ine' were determined in separate assays. Cyst(e)ine was calculated as ‘methionine plus cyst(e)ine' minus methionine. In whey protein which had reacted with oxidizing methyl linolenate, the bioavailable methionine content was not significantly reduced even though 82% of the methionine residues were present as methionine sulphoxide. In hydrogen peroxide-treated casein in which all methionine residues were oxidized to the sulphoxide, methionine sulphoxide was found to be 96% as utilizable as a methionine source to the rat. Free methionine sulphoxide was 87% utilizable. 5. Cyst(e)ine appeared to be as sensitive as lysine to reactions with lipid oxidation products. In whey protein which had reacted with oxidizing methyl linolenate, the bioavailabilities of cyst(e)ine, lysine, tryptophan and methionine were reduced by 28, 24, 11 and 8% respectively and true N digestibility by 9%. These results are discussed in relation to food product

    Survival Mechanisms Used by Some Leishmania Species to Escape Neutrophil Killing

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    Neutrophils are the most abundant leukocytes in human blood. Upon microbial infection, they are massively and rapidly recruited from the circulation to sites of infection where they efficiently kill pathogens. To this end, neutrophils possess a variety of weapons that can be mobilized and become effective within hours following infection. However, several microbes including some Leishmania spp. have evolved a variety of mechanisms to escape neutrophil killing using these cells as a basis to better invade the host. In addition, neutrophils are also present in unhealing cutaneous lesions where their role remains to be defined. Here, we will review recent progress in the field and discuss the different strategies applied by some Leishmania parasites to escape from being killed by neutrophils and as recently described for Leishmania mexicana, even replicate within these cells. Subversion of neutrophil killing functions by Leishmania is a strategy that allows parasite spreading in the host with a consequent deleterious impact, transforming the primary protective role of neutrophils into a deleterious one

    Formula milk supplementation on the postnatal ward: a cross-sectional analytical study

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    Breastfeeding rates are low in the UK, where approximately one quarter of infants receive a breastmilk substitute (BMS) in the first week of life. We investigated the reasons for early BMS use in two large maternity units in the UK, in order to understand the reasons for the high rate of early BMS use in this setting. Data were collected through infant feeding records, as well as maternal and midwife surveys in 2016. During 2016, 28% of infants received a BMS supplement prior to discharge from the hospital maternity units with only 10% supplementation being clinically indicated. There was wide variation in BMS initiation rates between different midwives, which was associated with ward environment and midwife educational level. Specific management factors associated with non-clinically indicated initiation of BMS were the absence of skin-to-skin contact within an hour of delivery (p = 0.01), and no attendance at an antenatal breastfeeding discussion (p = 0.01). These findings suggest that risk of initiating a BMS during postnatal hospital stay is largely modifiable. Concordance with UNICEF Baby Friendly 10 steps, attention to specific features of the postnatal ward working environment, and the targeting of midwives and mothers with poor educational status may all lead to improved exclusive breastfeeding rates at hospital discharge

    Stability of tryptophan during food processing and storage: 1. Comparative losses of tryptophan, lysine and methionine in different model systems

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    1. The stability of tryptophan was evaluated in several different food model systems using a chemical method (high pressure liquid chromatography after alkaline-hydrolysis) and rat assays. Losses of tryptophan were compared with the losses of lysine and methionine. 2. Whey proteins stored in the presence of oxidizing lipids showed large losses of lysine and extensive methionine oxidation but only minor losses of tryptophan as measured chemically. The observed decrease in bioavailable tryptophan was explained by a lower protein digestibility. 3. Casein treated with hydrogen peroxide to oxidize all methionine to methionine sulphoxide showed a 9% loss in bioavailable tryptophan. 4. When casein was reacted with caffeic acid at pH 7 in the presence of monophenol monooxygenase (tyrosinase; EC 1.14.18.l), no chemical loss of tryptophan occurred, although fluorodinitrobenzene-reactive lysine fell by 23%. Tryptophan bioavailability fell IS%, partly due to an 8% reduction in protein digestibility. 5. Alkali-treated casein (0.15 M-sodium hydroxide, 80°,4 h) did not support rat growth. Chemically-determined tryptophan, available tryptophan and true nitrogen digestibility fell 10, 46 and 23% respectively. Racemization of tryptophan was found to be 10% (D/(D+L)). 6. In whole-milk powder, which had undergone ‘early' or ‘advanced' Maillard reactions, tryptophan, determined chemically or in rat assays, was virtually unchanged. Extensive lysine losses occurred. 7. It was concluded that losses of tryptophan during food processing and storage are small and of only minor nutritional importance, especially when compared with much larger losses of lysine and the more extensive oxidation of methionin

    Labeling the human skeleton with 41Ca to assess changes in bone calcium metabolism

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    Bone research is limited by the methods available for detecting changes in bone metabolism. While dual X-ray absorptiometry is rather insensitive, biochemical markers are subject to significant intra-individual variation. In the study presented here, we evaluated the isotopic labeling of bone using 41Ca, a long-lived radiotracer, as an alternative approach. After successful labeling of the skeleton, changes in the systematics of urinary 41Ca excretion are expected to directly reflect changes in bone Ca metabolism. A minute amount of 41Ca (100nCi) was administered orally to 22 postmenopausal women. Kinetics of tracer excretion were assessed by monitoring changes in urinary 41Ca/40Ca isotope ratios up to 700days post-dosing using accelerator mass spectrometry and resonance ionization mass spectrometry. Isotopic labeling of the skeleton was evaluated by two different approaches: (i) urinary 41Ca data were fitted to an established function consisting of an exponential term and a power law term for each individual; (ii) 41Ca data were analyzed by population pharmacokinetic (NONMEM) analysis to identify a compartmental model that describes urinary 41Ca tracer kinetics. A linear three-compartment model with a central compartment and two sequential peripheral compartments was found to best fit the 41Ca data. Fits based on the use of the combined exponential/power law function describing urinary tracer excretion showed substantially higher deviations between predicted and measured values than fits based on the compartmental modeling approach. By establishing the urinary 41Ca excretion pattern using data points up to day 500 and extrapolating these curves up to day 700, it was found that the calculated 41Ca/40Ca isotope ratios in urine were significantly lower than the observed 41Ca/40Ca isotope ratios for both techniques. Compartmental analysis can overcome this limitation. By identifying relative changes in transfer rates between compartments in response to an intervention, inaccuracies in the underlying model cancel out. Changes in tracer distribution between compartments were modeled based on identified kinetic parameters. While changes in bone formation and resorption can, in principle, be assessed by monitoring urinary 41Ca excretion over the first few weeks post-dosing, assessment of an intervention effect is more reliable ∼150days post-dosing when excreted tracer originates mainly from bon

    Alginate inhibits iron absorption from ferrous gluconate in a randomized controlled trial and reduces iron uptake into Caco-2 cells

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    Previous in vitro results indicated that alginate beads might be a useful vehicle for food iron fortification. A human study was undertaken to test the hypothesis that alginate enhances iron absorption. A randomised, single blinded, cross-over trial was carried out in which iron absorption was measured from serum iron appearance after a test meal. Overnight-fasted volunteers (n=15) were given a test meal of 200g cola-flavoured jelly plus 21 mg iron as ferrous gluconate, either in alginate beads mixed into the jelly or in a capsule. Iron absorption was lower from the alginate beads than from ferrous gluconate (8.5% and 12.6% respectively, p=0.003). Sub-group B (n=9) consumed the test meals together with 600 mg calcium to determine whether alginate modified the inhibitory effect of calcium. Calcium reduced iron absorption from ferrous gluconate by 51%, from 11.5% to 5.6% (p=0.014), and from alginate beads by 37%, from 8.3% to 5.2% (p=0.009). In vitro studies using Caco-2 cells were designed to explore the reasons for the difference between the previous in vitro findings and the human study; confirmed the inhibitory effect of alginate. Beads similar to those used in the human study were subjected to simulated gastrointestinal digestion, with and without cola jelly, and the digestate applied to Caco-2 cells. Both alginate and cola jelly significantly reduced iron uptake into the cells, by 34% (p=0.009) and 35% (p=0.003) respectively. The combination of cola jelly and calcium produced a very low ferritin response, 16.5% (p<0.001) of that observed with ferrous gluconate alone. The results of these studies demonstrate that alginate beads are not a useful delivery system for soluble salts of iron for the purpose of food fortification
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