Elzbieta Kostyra

Institute of Animal Reproduction and Food Research of Polish Academy of Sciences, Olsztyn, Warmian-Masurian Voivodeship, Poland

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Publications (8)19.44 Total impact

  • Article: Impact of Maillard reaction on immunoreactivity and allergenicity of the hazelnut allergen Cor a 11.
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    ABSTRACT: Few studies exist on the influence of processing methods on structural changes and allergenic potential of hazelnut proteins. This study focused on the effect of glycation (Maillard reaction) on the immunoreactivity and degranulation capacity of the purified hazelnut 7S globulin, Cor a 11. After heating, the extent of the Maillard reaction, sensitivity to proteolysis, binding of human IgE or rabbit IgG, and degranulation capacity were analyzed. Changes in electrophoretic mobility, amount of free amino groups, and contents of bound sugar and fructosamine indicated that glycation of Cor a 11 occurred at all conditions. Glycation at 37 °C did not influence the specific IgG or IgE binding and was decreased after heating at 60 and 145 °C. Heating, with or without glucose, at 145 °C increased basophil degranulation capacity. The results suggest that glycation of Cor a 11 at 60 and 145 °C may decrease the IgE/IgG binding properties but not the degranulation capacity of basophils. This is possibly related to aggregation of the proteins as a result of the Maillard reaction.
    Journal of Agricultural and Food Chemistry 06/2011; 59(13):7163-71. · 2.82 Impact Factor
  • Article: Cow's-milk-induced infant apnoea with increased serum content of bovine β-casomorphin-5.
    Journal of pediatric gastroenterology and nutrition 06/2011; 52(6):772-5. · 2.18 Impact Factor
  • Article: The impact of pea protein hydrolysates on bacterial physiological activity--an in vitro study.
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    ABSTRACT: So far, food proteins have been perceived hitherto purely as a source of nutrients indispensable for maintaining life. However, latest findings strongly indicate that food proteins may release biologically active peptides in a consequence of enzymatic degradation. Such hydrolysates may be used as food components in order to beneficially influence human health. Additionally, such modified peptides may affect the balance of bacteria inhabiting human gastrointestinal tract and thus bring about health complication of the host. Although pea seeds are of significant nutritional value due to their high contents of proteins, carbohydrates and fibre, they are also responsible for health inconveniences resulting from their susceptibility to digestion and occurrence of antinutritional as well as allergic compounds. The enzymatic degradation may pass over these nutritional obstacles by liberating hydrolysates empowered not only to exert their impact on the human physiology but also on bacterial intestinal ecosystem. Therefore, the aim of this study was to evaluate the influence of pea protein hydrolysates on bacteria typical for the small intestine. Pea protein hydrolysates have proved to diversely modulate physiological activity of bacteria existing in different states. The observed detrimental effect on planktonic bacteria was abolished in the case of bacteria immobilized to the solid surfaces, confirming the protective effect of biofilms. Additionally, Lactobacilli displayed adaptive properties enabling them to utilize pea protein hydrolysates regardless their state of existence.
    International journal of food microbiology 06/2010; 140(2-3):263-70. · 3.01 Impact Factor
  • Article: Transport of micro-opioid receptor agonists and antagonist peptides across Caco-2 monolayer.
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    ABSTRACT: Milk is the source of beta-casomorphins--biologically active peptides with opioid activity--which are suspected to play various roles in the human body. The local influence of exogenous opioid peptides on gastrointestinal functions has been widely reported. After passing the gut barrier, beta-casomorphins may affect the functions of immunological system, as well as dopaminergic, serotoninergic and GABA-ergic systems in brain, regulate the opioid receptor development and elicit behavioral effects. However, possibilities and mechanisms of the intestinal transport of beta-casomorphins in human body in vivo have not been reported so far. In our research, the transepithelial transport of micro-opioid receptor agonists--human beta-casomorphin-5 and 7(BCM5, BCM7) and antagonist--lactoferroxin A (LCF A) have been investigated using Caco-2 monolayer. In order to determine the pathway of investigated peptide transport across Caco-2 monolayer, two directions of the transport (apical to basolateral and basolateral to apical) have been studied. All investigated peptides were transported across the human intestinal cell line Caco-2 and the curves of cumulative amount of transported peptides in time were linear in each case. In addition, the hydrolysis of beta-casomorphins during 60 min of experiment by dipeptidyl peptidase IV was observed. The data suggest the possibility of transport of opioid peptides derived from food across human intestinal mucosa.
    Peptides 07/2008; 29(6):1042-7. · 2.43 Impact Factor
  • Article: Content of beta-casomorphins in milk of women with a history of allergy.
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    ABSTRACT: The prevalence of food allergies increased over the past decade. Most symptoms of food allergy appear during the first 2 yr of life. The aim of this study was to determine the beta-casomorphin-5 and -7 (BCMs) in colostrum and milk of 12 breast-feeding women with a history and clinical manifestation of food allergy. The results were compared with the data obtained from a control group of healthy age-matched breast-feeding women. The level of BCM in women with food allergy was constant during lactation, whereas the highest level of opioid peptides was found in colostrums of healthy women with a subsequent rapid decrease in mature milk. These differences in BCMs profile between allergic and healthy breast-feeding women suggest that BCM content in the human milk may be an indicator of allergic conditions.
    Pediatric Allergy and Immunology 02/2008; 19(7):587-91. · 2.46 Impact Factor
  • Article: Changes of beta-casomorphin content in human milk during lactation.
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    ABSTRACT: Milk is the best, complete food important for the development and nourishment of a neonate. Except for nutrients, milk contains biologically active opioid peptides derived from beta-casein, named beta-casomorphins (BCMs), which can exert effects in the gastrointestinal tract as well as in the whole body of neonates. The content of beta-casomorphins in human milk during maturation phases has not been studied so far. The aim of this study was to determine the content of beta-casomorphin-5 and -7 in human milk in different phases of lactation. A significantly higher concentration of both beta-casomorphins was found in colostrum than in mature milk. The concentration of beta-casomorphin in milk collected in the second month of lactation was similar to the level obtained in the fourth month of lactation. The content of beta-casomorphins in human milk was observed with the period of lactation. The level of opioid peptides may depend on the function of these peptides in neonate's body and may be associated with the maturation process.
    Peptides 11/2007; 28(10):1982-6. · 2.43 Impact Factor
  • Article: Serum activity of dipeptidyl peptidase IV (DPPIV; EC 3.4.14.5) in breast-fed infants with symptoms of allergy.
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    ABSTRACT: Beta-casomorphins, opioid peptides present in mother's milk, are a good substrate for DPPIV (EC 3.4.14.5) which is a major factor limiting the half-life of biologically active peptides. Serum DPPIV activity of two groups of infants (healthy and atopic dermatitis) and contents of beta-casomorphin-5 and -7 in their mothers' milk were determined in the study. We have found correlation between those two parameters in the group of children with atopic dermatitis syndromes, while no such a correlation was found in the control group.
    Peptides 04/2007; 28(3):678-82. · 2.43 Impact Factor
  • Article: Polymorphism of bovine beta-casein and its potential effect on human health.
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    ABSTRACT: Proteins in bovine milk are a common source of bioactive peptides. The peptides are released by the digestion of caseins and whey proteins. In vitro the bioactive peptide beta-casomorphin 7 (BCM-7) is yielded by the successive gastrointestinal proteolytic digestion of bovine beta-casein variants A1 and B, but this was not seen in variant A2. In hydrolysed milk with variant A1 of beta-casein, BCM-7 level is 4-fold higher than in A2 milk. Variants A1 and A2 of beta-casein are common among many dairy cattle breeds. A1 is the most frequent in Holstein-Friesian (0.310-0.660), Ayrshire (0.432-0.720) and Red (0.710) cattle. In contrast, a high frequency of A2 is observed in Guernsey (0.880-0.970) and Jersey (0.490-0.721) cattle. BCM-7 may play a role in the aetiology of human diseases. Epidemiological evidence from New Zealand claims that consumption of beta-casein A1 is associated with higher national mortality rates from ischaemic heart disease. It seems that the populations that consume milk containing high levels of beta-casein A2 have a lower incidence of cardiovascular disease and type 1 diabetes. BCM-7 has also been suggested as a possible cause of sudden infant death syndrome. In addition, neurological disorders, such as autism and schizophrenia, seem to be associated with milk consumption and a higher level of BCM-7. Therefore, careful attention should be paid to that protein polymorphism, and deeper research is needed to verify the range and nature of its interactions with the human gastrointestinal tract and whole organism.
    Journal of applied genetics 02/2007; 48(3):189-98. · 1.66 Impact Factor