Allergenicity of Proteolytic Hydrolysates of the Soybean 11S Globulin

Lee, H.-W.; Keum, Eun-Hee; Lee, S.-J.; Sung, Dong-Eun; Chung, Doug Young; Lee, S.-I.; Oh, Sangsuk

doi:10.1111/j.1750-3841.2007.00307.x

Cited by 38 publications

(24 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, other studies [25,26,27] have shown that Ara h 3 basic subunits may be important allergenic peptides. The resistance of the 11S globulin basic subunit to enzymatic hydrolysis has been reported previously in soybeans [28]. …”

Section: Discussionmentioning

confidence: 97%

Influence of Enzymatic Hydrolysis on the Allergenicity of Roasted Peanut Protein Extract

Cabanillas

Pedrosa

Rodríguez

et al. 2011

Int Arch Allergy Immunol

View full text Add to dashboard Cite

Background: Peanut allergy is recognized as one of the most severe food allergies. Some studies have investigated the effects of enzymatic treatments on the in vitro immunological reactivity of members of the Leguminosae family, such as the soybean, chickpea and lentil. Nevertheless, there are only a few studies carried out with sera from patients with a well-documented allergy. Methods: Roasted peanut protein extract was hydrolyzed by the sequential and individual action of 2 food-grade enzymes, an endoprotease (Alcalase) and an exoprotease (Flavourzyme). Immunoreactivity to roasted peanut extract and hydrolyzed samples was evaluated by means of IgE immunoblot, ELISA and 2-dimensional electrophoresis using sera from 5 patients with a clinical allergy to peanuts and anti-Ara h 1, anti-Ara h 2 and anti-Ara h 3 immunoblots. Results: Immunoblot and ELISA assays showed an important decrease of IgE reactivity and Ara h 1, Ara h 2 and Ara h 3 levels in the first 30 min of hydrolyzation with Alcalase. In contrast, individual treatment with Flavourzyme caused an increase in IgE reactivity detected by ELISA at 30 min and led to a 65% inhibition of IgE reactivity at the end of the assay (300 min). Ara h 1 and the basic subunit of Ara h 3 were still recognized after treatment with Flavourzyme for 300 min. Conclusion: Hydrolysis with the endoprotease Alcalase decreases IgE reactivity in the soluble protein fraction of roasted peanut better than hydrolysis with the exoprotease Flavourzyme.

show abstract

Section: Discussionmentioning

confidence: 97%

Influence of Enzymatic Hydrolysis on the Allergenicity of Roasted Peanut Protein Extract

Cabanillas

Pedrosa

Rodríguez

et al. 2011

Int Arch Allergy Immunol

View full text Add to dashboard Cite

show abstract

“…The IgE binding capacity of soy glycinin is reported not to be affected by heating [17], while sequential hydrolysis by pepsin and chymotrypsin is reported to result in peptides of 20 kDa and smaller, with a 20 kDa peptide still being able to bind IgE [18]. The effects of heating and digestion on the IgE binding capacity of Ara h 3 have not been investigated yet.…”

Section: Introductionmentioning

confidence: 96%

Legumin allergens from peanuts and soybeans: Effects of denaturation and aggregation on allergenicity

Boxtel

Broek²,

Koppelman

et al. 2008

Molecular Nutrition Food Res

View full text Add to dashboard Cite

Legumin proteins Ara h 3 from peanuts and glycinin from soybeans are increasingly described as important allergens. The stability of an allergen's IgE binding capacity towards heating and digestion is considered an important characteristic for food allergens. We investigated the effects of heating and digestion on the IgE binding of Ara h 3 and glycinin. Both proteins are relatively stable to denaturation, having denaturation temperatures ranging from 70 to 92 degrees C, depending on their quaternary structure and the ionic strength. Aggregates were formed upon heating, which were partly soluble for glycinin. Heating slightly decreased the pepsin digestion rate of both allergens. However, heating did not affect the IgE binding capacity of the hydrolyzates, as after only 10 min of hydrolysis no IgE binding could be detected any more in all samples. Peanut allergen Ara h 1, when digested under equal conditions, still showed IgE binding after 2 h of hydrolysis. Our results indicate that the IgE binding capacity of legumin allergens from peanuts and soybeans does not withstand peptic digestion. Consequently, these allergens are likely unable to sensitize via the gastro-intestinal tract and cause systemic food allergy symptoms. These proteins might thus be less important allergens than was previously assumed.

show abstract

“…Although most food allergens maintain their activity after passing through the digestive tract, the relationship between food allergenicity and digestibility is still unclear. Stability to denaturation and proteolysis, and potential for aggregation seem to be important factors, as well as allergen concentration (Lee et al, 2007;Van Boxtel et al, 2008).…”

Section: Allergenicity Of Pulse Proteinsmentioning

confidence: 99%

Role of pulses in nutraceuticals

Carbonaro

2011

Pulse Foods

View full text Add to dashboard Cite

Allergenicity of Proteolytic Hydrolysates of the Soybean 11S Globulin

Cited by 38 publications

References 26 publications

Influence of Enzymatic Hydrolysis on the Allergenicity of Roasted Peanut Protein Extract

Influence of Enzymatic Hydrolysis on the Allergenicity of Roasted Peanut Protein Extract

Legumin allergens from peanuts and soybeans: Effects of denaturation and aggregation on allergenicity

Role of pulses in nutraceuticals

Contact Info

Product

Resources

About