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1

Reduction of milk allergenicity using new synthesized Cu(II) complex as artificial protease

100%
Divsalar A., Saboury A. A., Mansouri-Torshizi H.
Polish Journal of Food and Nutrition Sciences
|
2011
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tom 61
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nr Suppl.1
2
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
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Effect of acylation and enzymatic modification on pea proteins allergenicity

100%
Szymkiewicz A., Jedrychowski L.
Polish Journal of Food and Nutrition Sciences
|
2008
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tom 58
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nr 3
In the study chemical modifications (acetylation or succinylation) and enzymatic hydrolysis (with Alcalase) were applied in order to reduce the allergenicity of particular pea proteins. Application of Alcalase after acylation lowered the immunoreactive properties of pea vicilin from 14-17% down to 2-2.5% as compared to that of the native fraction. Under these conditions, the immunoreactivity of legumin and albumins was reduced by nearly 100%. Proteolysis of pea proteins under conditions optimal for Alcalase decreased the immunoreactivity of vicilin to about 24%. Application of acetic anhydrides for further modification led to lowering their level to 6% and 9%, during acetylation and succinylation, respectively. The immunoreactivity of pea legumin and albumins was reduced down to 1-3%. The lower immunoreactive properties of particular pea proteins do not correspond with lower allergenicity of total proteins. Of all the applied methods acetylation of previously hydrolysed proteins proved to be the most effective; it resulted in about 70% allergenicity decrease (on the average) of thus modified samples as compared to native pea proteins. Yet, the reaction showed an individual character and may be different in individual patients.
3
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Isolation and purification of individual gliadin proteins by preparative acid polyacrylamide gel electrophoresis [A-PAGE] for allergenic research

100%
Waga J., Zientarski J.
Polish Journal of Food and Nutrition Sciences
|
2007
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tom 57
|
nr 1
Gliadins are a large and complex group of proteins, consisting of dozens to hundreds of unique polypeptides in any wheat cultivar. Individual gliadins differ in molecular weight, isoelectric point, and amino acid sequences, making their analyses especially difficult. We here used preparative polyacrylamide gel electrophoresis in acidic conditions to fractionate gliadins of the cultivar Fraza. Resulting fractions were then analysed by ELISA to test their immunoreactive properties with antigliadin polyclonal antibodies. Preparative electrophoresis yielded 60 aliquots, of which 15 contained single proteins. Separated gliadins differed in immunoreactive properties: antigliadin antibodies bound stronger to a and b gliadins, while the immunoenzymatic reaction with g and w-gliadins was much weaker.
4
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Peanut allergenicity and cross-reactivity with pea proteins in the in vivo model

80%
Szymkiewicz A., Chudzik-Kozlowska J.
Polish Journal of Food and Nutrition Sciences
|
2013
|
tom 63
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nr 1
The aim of the study was to analyse the potential pea-peanut cross-reactivity using the mice BALB/c as a biological in vivo model in the research on immune response to peanut proteins (PnE). BALB/c mice were three-fold sensitised (on days 1, 7, and 21) by oral or intraperitoneal (IP) administration of PnE in 0.5 mg or 1 mg dose, with or without adjuvant – aluminum hydroxide gel (Alum). Serum immunoglobulins (IgE, IgG, IgG1 and IgG2a) and level of cytokines (IL-4, IL-10, IFN- γ), secreted by the isolated lymphocytes were examined. The highest increase in total IgE and peanut-specific IgG1 was noted in the group sensitised by IP administration of PnE in the presence of Alum. Lymphocytes from peanut-sensitised (with and without Alum) mice showed a significantly high level of IL-4 and this cytokine was secreted to a much higher extent as compared to IFN-γ. Stimulation of a culture of lymphocytes with pea proteins resulted in high IFN-γ secretion. A weak reaction of peanut-specific IgG1 present in mice serum with pea globulins (vicilin – PV and legumin – PL) can suggest that the cross-reactivity between peanut and pea proteins results from the presence of proteins other than 7S and 11S globulins. Due to the demonstrated low cross-reactivity between peanut proteins and pea globulins, the possibility of applying pea proteins in peanut-allergy immunotherapy may be suggested.
5
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Allergenicity of lupine proteins - a review

80%
Loza A., Lampart-Szczapa E.
Polish Journal of Food and Nutrition Sciences
|
2008
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tom 58
|
nr 3
In Europe, the application of lupine seeds to produce food has increased significantly in recent years. Lupine (flour, seeds or dust) can induce different allergic responses. Consumption of lupine-fortified products may also provoke allergy syndromes. This article reviews the adverse reactions to lupine, after various contacts with this plant, including eating lupine products and seeds. It discusses cases which confirm properties of lupine protein as a primary allergen. It describes lupine protein cross-reactivity and the modifying effect of thermal processes on lupine protein.
6

Projekt zintegrowany UE 'ISAFRUIT'. Zwiekszenie spozycia owocow poprzez interdyscyplinarne podejscie prowadzace do uzyskania wysokiej jakosci produktu za pomoca zrownowazonych i bezpiecznych dla srodowiska metod. Cz.2

61%
Plocharski W.
Przemysł Fermentacyjny i Owocowo-Warzywny
|
2007
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tom 51
|
nr 07-08
14
EU "ISAFRUIT" Project covers different areas of research including investigation of effects of fruit consumption on well being, human health and obesity. Allergy induced by fruit consumption is also covered beside investigation of the risk to human health and environment of new methods of fruit production. Pillar covering fruit processing has been divided into 4 work packages (WP's), which share common idea of preservation in processed products, to the highest level possible, components beneficial for human health that are found in raw material. In the WP covering minimally processed fruit various techniques are applied including high pressure and microwaves to increase fruit safety. Direct juices, nectars and drinks are also object of research of this pillar as healthy products with high export potential. Selection of raw material for direct juice production and improvement of technology has been foreseen. The outcome of the project will also be new dried fruit products with functional properties. Proposal to utilize waste products (fruit pomaces) will also be given. Within the project several new approaches to fruit production methods and product management are developed, including Decision Support System, which will contribute to improvement of fruit quality supplied to the consumer. A new pesticide application system is under development, which will allow higher protection of environment. Beside applied research also basic research will be conducted within the project covering identification and mapping of the major genes responsible for fruit quality and development of safe and efficient transgenic techniques applicable to quality-fruit production. Knowledge created within the project will be disseminated using various tools such as internet, conferences, scientific publications and popular articles to inform European citizens. This should contribute, according to the project premises, to increased consumption of fruits and improvement of human well being and health.
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