Cu, Fe, Mn and Zn distribution in protein fractions of Brazil-nut, cupuassu seed and coconut pulp by solid-liquid extraction and electrothermal atomic absorption spectrometry

Naozuka, Juliana; Oliveira, Pedro Vitoriano de

doi:10.1590/s0103-50532007000800015

Cited by 37 publications

(22 citation statements)

References 26 publications

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“…It is well discussed in the literature 12,13 that the extractants water, NaCl, ethanol and NaOH promoted the separation of different groups of proteins: albumins, globulins, prolamins and glutelins, respectively. 12,13 The total protein concentration obtained by the masses sum of all extracts revealed that cooking promoted a sensible decrease in the protein content, mainly in the globulins fraction, when compared to the uncooked beans. Previous investigations showed that the total protein concentration ranged from 22.57 to 24.42 g per 100 g and from 23.25 to 26.29 g per 100 g for raw and cooked beans, respectively.…”

Section: Cooking Effects On Protein Concentrationmentioning

confidence: 99%

Cooking effects on iron and proteins content of beans (Phaseolus Vulgaris L.) by GF AAS and MALDI-TOF MS

Naozuka¹,

Oliveira²

2012

J. Braz. Chem. Soc.

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Os efeitos do cozimento doméstico na distribuição de proteínas, compostos orgânicos e Fe em feijão (Phaseolus vulgaris L.) foram investigados. Extração seqüencial com diferentes agentes extratores (mistura de metanol e clorofórmio 1:2 v/v, água, NaCl, etanol e NaOH) foi usada para extrair lipídeos, albuminas, globulinas, prolaminas e glutelinas, respectivamente. A determinação de Fe por espectrometria de absorção atômica com forno de grafite (GF AAS), de proteínas pelo método de Bradford e compostos orgânicos por espectrometria de massas por tempo de vôo acoplada à ionização dessortiva de matriz por laser (MALDI-TOF MS) foram feitas nesse trabalho. Altas concentrações de albuminas, globulinas e glutelínas foram encontradas em feijão cru, enquanto que em grãos cozidos, albuminas e glutelínas foram os principais tipos de proteínas. Os espectros de MALDI-TOF MS do feijão cru e cozido revelaram que o cozimento doméstico alterou os pesos moleculares dos compostos orgânicos, uma vez que nos grãos cozidos foram encontrados compostos entre 2 e 3,5 kDa, os quais não estavam presentes no feijão cru. Além disso, no feijão cozido foi também observada a presença de quatro compostos de alto peso molecular (12-16 kDa), sendo que em grãos crus há somente um (ca.15,2 kDa). Nos grãos crus foi possível observar que Fe está principalmente associado a albuminas, globulinas e glutelínas. Para os grãos cozidos, Fe está presente em alta concentração em albuminas e globulinas.The effects of domestic cooking on proteins, organic compounds and Fe distribution in beans (Phaseolus vulgaris L.) were investigated. Sequential extraction with different extractant solutions (mixture of methanol and chloroform 1:2 v/v, water, 0.5 mol L -1 NaCl, 70% v/v ethanol and 0.5 mol L -1 NaOH) were used for extracting lipids, albumins, globulins, prolamins and glutelins, respectively. Iron determination by graphite furnace atomic absorption spectrometry (GF AAS), proteins by Bradford method and organic compounds by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) were carried out in this work. High concentration of albumins, globulins and glutelins were found in raw beans, while in the cooked beans, albumins and glutelins are main proteins types. The MALDI-TOF MS spectra of raw and cooked beans revealed that the domestic cooking altered the molecular weight of the organic compounds, since that in the cooked beans were found compounds between 2 and 3.5 kDa, which were not presented in the raw beans. Besides this, in cooked beans were also observed the presence of four compounds of high molecular weight (12-16 kDa), being that in the raw grains there is only one (ca. 15.2 kDa). In raw grains is possible to observe that Fe is mainly associated to albumins, globulins and glutelins. For cooked grains, Fe is associated to albumins and globulins.

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Section: Cooking Effects On Protein Concentrationmentioning

confidence: 99%

Cooking effects on iron and proteins content of beans (Phaseolus Vulgaris L.) by GF AAS and MALDI-TOF MS

Naozuka¹,

Oliveira²

2012

J. Braz. Chem. Soc.

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“…The metal contents of the digested samples were determined in an Analytikjena AG, AAS ZEEnit 60 instrument. Iron, copper, and zinc were detected at 324.8, 248.3, and 213.9 nm, respectively (30).…”

Section: S Cerevisiae Strains and Growth Conditions-mentioning

confidence: 99%

Superoxide Dismutase 1-mediated Production of Ethanol- and DNA-derived Radicals in Yeasts Challenged with Hydrogen Peroxide

Ogusucu

Rettori

Netto

et al. 2009

Journal of Biological Chemistry

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Peroxiredoxins are receiving increasing attention as defenders against oxidative damage and sensors of hydrogen peroxide-mediated signaling events. In the yeast Saccharomyces cerevisiae, deletion of one or more isoforms of the peroxiredoxins is not lethal but compromises genome stability by mechanisms that remain under scrutiny. Here, we show that cytosolic peroxiredoxin-null cells (tsa1⌬tsa2⌬) are more resistant to hydrogen peroxide than wildtype (WT) cells and consume it faster under fermentative conditions. Also, tsa1⌬tsa2⌬ cells produced higher yields of the 1-hydroxyethyl radical from oxidation of the glucose metabolite ethanol, as proved by spin-trapping experiments. A major role for Fenton chemistry in radical formation was excluded by comparing WT and tsa1⌬tsa2⌬ cells with respect to their levels of total and chelatable metal ions and of radical produced in the presence of chelators. The main route for 1-hydroxyethyl radical formation was ascribed to the peroxidase activity of Cu,Znsuperoxide dismutase (Sod1), whose expression and activity increased ϳ5-and 2-fold, respectively, in tsa1⌬tsa2⌬ compared with WT cells. Accordingly, overexpression of human Sod1 in WT yeasts led to increased 1-hydroxyethyl radical production. Relevantly, tsa1⌬tsa2⌬ cells challenged with hydrogen peroxide contained higher levels of DNA-derived radicals and adducts as monitored by immuno-spin trapping and incorporation of 14 C from glucose into DNA, respectively. The results indicate that part of hydrogen peroxide consumption by tsa1⌬tsa2⌬ cells is mediated by induced Sod1, which oxidizes ethanol to the 1-hydroxyethyl radical, which, in turn, leads to increased DNA damage. Overall, our studies provide a pathway to account for the hypermutability of peroxiredoxin-null strains.Living organisms are constantly exposed to oxygen-and nitrogen-derived reactive species that are produced by normal metabolic activity and in response to external stimuli. To protect themselves against the toxicity of these species, aerobic organisms have evolved a range of defense mechanisms (1). Among these, a family of cysteine-based peroxidases, currently named peroxiredoxins, has attracted considerable attention because of its ubiquity and versatility. These enzymes have been shown to detoxify hydrogen peroxide, organic peroxides and peroxynitrite through oxidation of their reactive cysteine residues, which are recycled back by reducing equivalents provided by thioredoxin and other thiol-electron donors (reviewed in Refs. 2-5). In addition to detoxifying peroxides, specific peroxiredoxins have been shown to act as molecular chaperones (6, 7) and to play roles in regulating hydrogen peroxide-mediated cell signaling events (3,8,9).Many organisms have multiple peroxiredoxins. Six peroxiredoxins have been identified in human cells, and five in the yeast Saccharomyces cerevisiae. Peroxiredoxin isoforms are distributed to different locations within the cell, and two of the yeast peroxiredoxins, Tsa1 and Tsa2, are cytosolic (10). Tsa1 was the first peroxiredox...

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“…and Zn 2? (Naozuka and Oliveira 2007 Fig. 4 In vitro digestibility of native and recombinant proteins in SGF.…”

Section: Lipid Metal-binding Propertiesmentioning

confidence: 99%

Ber e 1 protein: the versatile major allergen from Brazil nut seeds

2011

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Due mainly to its extremely high content of sulphur amino acids, Ber e 1 protein, the major allergen from Brazil nut, has attracted much scientific and press attention. Ber e 1 was the main target protein in early biotechnology transgenic work, in early processing studies of plant storage proteins, in plant vacuolar targeting studies and as the main protein in early nutritional supplementation experiments. Ber e 1 was also one of the first food allergens to be unintentionally transferred from one plant to another and was involved in the first reported case of systemic allergic reaction caused by a food allergen transferred in semen. In this review, many of the Ber e 1 unique biotechnological and structural functions are discussed with a particular emphasis on its use as model protein for studies of intrinsic allergenicity of food proteins.

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Cu, Fe, Mn and Zn distribution in protein fractions of Brazil-nut, cupuassu seed and coconut pulp by solid-liquid extraction and electrothermal atomic absorption spectrometry

Cited by 37 publications

References 26 publications

Cooking effects on iron and proteins content of beans (Phaseolus Vulgaris L.) by GF AAS and MALDI-TOF MS

Cooking effects on iron and proteins content of beans (Phaseolus Vulgaris L.) by GF AAS and MALDI-TOF MS

Superoxide Dismutase 1-mediated Production of Ethanol- and DNA-derived Radicals in Yeasts Challenged with Hydrogen Peroxide

Ber e 1 protein: the versatile major allergen from Brazil nut seeds

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