Influence of physicochemical conditions and technological treatments on the iron binding capacity of egg yolk phosvitin

Castellani, Oscar; Guérin-Dubiard, Catherine; David-Briand, Elisabeth; Anton, Marc

doi:10.1016/j.foodchem.2003.08.002

Cited by 79 publications

(71 citation statements)

References 26 publications

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“…However, conalbumin (ovotransferin) binds iron depending on albumen pH [7] and also other metals, such as Cu, Zn, Al, Cd, Co, Mn, Cr [8] . Phosphoprotein, such as egg yolk phosvitin binds almost the whole iron in egg content [9] . Trace elements, such as Cr, Ni, I, Zn can be bound by some lipid compounds of egg yolk [8,10] and many others can be incorporated in eggshells or eggshell membranes [11,12] and these processes are very complicated biochemically [13,14] .…”

Section: Introductionmentioning

confidence: 99%

Effect of Dietary Humic Preparations on the Content of Trace Elements in Hensâ€™ Eggs

Dobrzański¹,

Górecki²,

Chojnacka³

et al. 2007

American J. of Agricultural and Biological Sciences

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Mineral-humic preparations Humokarbowit (HKW) and Humobentofet (HBF) were used in feeding of reproductive laying hens Lohmann Brown. The effect of these preparations on microelement composition of eggs was investigated. The content of microelements in hens diet, egg albumen and eggshell was determined by ICP-MS technique and relative bioaccumulation coefficient (RBC) was evaluated. The humic preparations significantly increased selenium and decreased molybdenum concentration in egg albumen. Increase of selenium and iron content in egg yolk and increase of iron concentration in eggshells was observed. The preparations did not influence the content of such elements as Cr, Co, Cu, I, Mn, Zn. The highest levels of RBC were found for selenium and iodine and the lowest for manganese.

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Section: Introductionmentioning

confidence: 99%

Effect of Dietary Humic Preparations on the Content of Trace Elements in Hensâ€™ Eggs

Dobrzański¹,

Górecki²,

Chojnacka³

et al. 2007

American J. of Agricultural and Biological Sciences

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“…However, a subunit of casein contains only 1 to 13 phosphoserine residues to stabilize the amorphous calcium phosphate, while an egg yolk protein molecule (phosvitin) contains approximately 120 phosphoserine residues, suggesting that several phosphopeptides with different sizes capable of binding and releasing calcium ions can form from phosvitin [72]. The granular fraction of egg yolk (after centrifugation, 10,000g, 30 min) is composed of phosvitin (60%) and lipovitelin.…”

Section: Bioactive Glycopeptides and Phosphopeptidesmentioning

confidence: 99%

“…The vast majority of the studies have been conducted with milk proteins. Pihlanto [53] described 2 peptides with hypocholesterolemic action resulting from hydrolysis of β-lactoglobulin by trypsin, Ile-Ile-Ala-Glu-Lys (β-Lg, f: [71][72][73][74][75] and Ala-Leu-Pro-Met-His (β-Lg, f: 142-146), with proven action in vitro, in cell cultures and in animal model, both receiving the name of lactostatin. The β-lactostatin (Ile-Ile-Ala-Glu-Lys) caused decrease of micellar cholesterol of intestinal environment reducing its absorption.…”

Section: Antihyperlipidemic and Antithrombotic Peptidesmentioning

confidence: 99%

Food Proteins and Bioactive Peptides, Functional Diets

Sgarbieri¹,

Armadas²

2017

FSN

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Throughout the second half of the last century and early this century the concept of the biological function of food proteins has changed significantly. While in the past the food proteins were regarded only as macronutrients capable of providing the amino acids to form the protein component of organs and tissues, also participating in the generation of metabolic energy for the normal functioning of living organisms, today it is known that certain proteins present in food, as well as fragments or peptides derived thereof, may participate in the general metabolism in a much more interactive manner, through bioactivities that go far beyond the nutritional functions that had been established by the end of the first half of the prior century.By making an analogy with the aeronautical activity we can say that in the past the food proteins functioned as black boxes holding numerous important pieces of information, which research and technology have only revealed, in part, in recent decades. In this period it Received: August 07, 2017; Accepted: September 12, 2017; Published: September 26, 2017 was found that certain proteins present in foods are naturally bioactive, and can be absorbed from the Gastrointestinal System (GIS) in their intact or slightly modified form and exercise specific bioactivities in the systemic metabolism [1], or, in addition, resist the action of digestive enzymes exercising different bioactivities in the gastrointestinal system [2]. Even more interesting were the findings that food proteins, of both plant and animal origin, contain, in their primary structures, specific amino acid sequences in their polypeptide chains, which when cleaved in the form of peptides by proteolytic enzymes or by specific chemical reagents may exercise diverse bioactivities that were latent in the original structure of the protein from which they originated.Bioactive peptides have been obtained from precursor proteins through the use of methodologies that have reached a high degree of sophistication and complexity, such as: (a) enzymatic hydrolysis by digestive enzymes; (b) proteolysis of the protein source by enzymes derived from microorganisms or plants; (c) fermentation process using culture with high proteolytic power and specificity. The bioactive potential of the peptides originating from the proteolysis of food proteins can be explored in the integral hydrolysates, produced in special conditions. However, in the current literature there are numerous research works and literature reviews emphasizing the importance of the isolation, purification, characterization, study of mechanisms and impact of these peptides on human health [3][4][5][6][7][8]. Production and Processing of Bioactive Peptides Derived from Food ProteinsA large number of plants and animals have been object of study as source of Bioactive Peptides (BAPs). Several studies were conducted, particularly with milk proteins [9,10], eggs [11,12], and muscle proteins from pigs [13], cattle [14], poultry [15], and fish [16]. BAPs have been obtained from...

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“…Estévez and Cava (2004) reported that the amount of free iron is increased by cooking and storage, and the highest concentrations are found in meat that is stored after being cooked. Importantly, Castellani et al (2004) found that phosvitin maintained a high iron binding capacity when it was treated by thermal (90 o C) or high pressure processing (600 Mpa). For these reasons, the extracted phosvitin from egg yolk could be used as a valuable antioxidative reagent in processed meat products which are subject to heat and storage before consumption.…”

Section: Tbars Values Of the Ground Beefmentioning

confidence: 99%

Elucidation of Antioxidant Activity of Phosvitin Extracted from Egg Yolk using Ground Meat

Jung¹,

Jo²,

Kang³

et al. 2012

Korean Journal for Food Science of Animal Resources

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AbastractPhosvitin was extracted from a chicken egg yolk and the iron-binding, along with antioxidative activity of the extracted phosvitin, was determined after mixing with ground beef at the concentrations of 100 and 500 mg/kg of meat. The electrophoretic pattern of the extracted phosvitin on SDS-PAGE was found to be identical to that of the standard phosvitin. The extracted phosvitin at 1,000 µg/mL showed an ability to bind approximately 65% of the iron in a 3 mM iron solution. Lipid oxidation was inhibited in the ground beef mixed with 500 mg/kg of the extracted phosvitin, during storage at 4o C compared to that of the control (p<0.05). Additionally, color stability of ground beef containing the extracted phosvitin was enhanced (p<0.05). The pH, cooking loss, texture, and sensory properties of the ground beef were not affected, by adding up to 500 mg/kg of the extracted phosvitin. This result suggests that the phosvitin extracted from egg yolk could be used as an antioxidant reagent. In particular, phosvitin would be more amenable for use in meat products because it is a natural protein derived from animal products.

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Influence of physicochemical conditions and technological treatments on the iron binding capacity of egg yolk phosvitin

Cited by 79 publications

References 26 publications

Effect of Dietary Humic Preparations on the Content of Trace Elements in Hensâ€™ Eggs

Effect of Dietary Humic Preparations on the Content of Trace Elements in Hensâ€™ Eggs

Food Proteins and Bioactive Peptides, Functional Diets

Elucidation of Antioxidant Activity of Phosvitin Extracted from Egg Yolk using Ground Meat

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