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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

tom 58

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.

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

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.

Ograniczanie wyników

2 Polish Journal of Food and Nutrition Sciences

2 Szymkiewicz A.

1 Chudzik-Kozlowska J.

1 Jedrychowski L.

1 2013

1 2008

Wyniki wyszukiwania

Effect of acylation and enzymatic modification on pea proteins allergenicity

Peanut allergenicity and cross-reactivity with pea proteins in the in vivo model