Reduction of Ovomucoid Immunogenic Activity on Peptic Fragmentation and Heat Denaturation

Matsuda, Tsukasa; Tsuruta, Kazuko; Nakabe, Yumiko; Nakamura, Ryô

doi:10.1080/00021369.1985.10867063

Cited by 2 publications

(4 citation statements)

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“…Reduced allergenicity in vivo Arita et al (2001) although precipitation was formed when stopping simulated gastric digestion. Matsuda, Tsuruta, Nakabe, and Nakamura (1985) found that pepsin hydrolysis followed by boiling for 30min could generate ovomucoid with a reduced in vivo allergenicity. Enzymatic hydrolysis has been reported to reduce IgE-binding capacity of egg white, either in the absence or presence of egg yolk.…”

Section: Processing Condition Allergenicity Change Referencesmentioning

confidence: 99%

“…Reduced allergenicity in vivo Matsuda et al (1985) Ovalbumin Gastric digestions: conducted at pH 2.0 at 37°C for 60 min, followed by duodenal digestions: conducted at pH 6.5 at 37°C for either 30 or 60 min Reduced IgE-binding capacity Lysozyme Gastric digestions: conducted at pH 2.0 at 37°C for 60 min, followed by duodenal digestions: conducted at pH 6.5 at 37°C for either 30 or 60 min Higher IgE-binding capacity after gastric digestions (pH adjustment before duodenal digestion leads to lysozyme precipitation) Jiménez-Saiz, Martos et al (2011) Egg white Chymotrypsin/pepsin at 1.7:1, pretreating for 3.16 hr and digesting for 3 hr…”

Section: Processing Condition Allergenicity Change Referencesmentioning

confidence: 99%

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Can food processing produce hypoallergenic egg?

Liang

Xing

et al. 2020

Journal of Food Science

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Eggs and their derived products are common foods that can induce food allergic reaction, especially in children. The reported incidence of egg allergy is 1% to 2%, and its prevalence has rapidly increased in recent years. Currently, there is no approved treatment for it. The clinical guidance for this adverse food reaction is the complete elimination of egg (and their derived products) from diet, which is difficult due to the wide use of egg ingredients in food industry. Food processing methods can affect the conformational and/or linear epitopes of allergens and may change the allergenicity of egg. Thermal treatment and various other processing methods based on the enzymatic hydrolysis and irradiation have been found useful in reducing allergenicity of certain egg allergens. However, processed egg proteins can also show an increased allergenicity after treatment and the correct pattern to follow for the generation of hypoallergenic products remains unclear. This review explores the influence of processing methods on egg allergenicity and reports the best options for the generation of hypoallergenic egg products to date.

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Section: Processing Condition Allergenicity Change Referencesmentioning

confidence: 99%

Section: Processing Condition Allergenicity Change Referencesmentioning

confidence: 99%

Can food processing produce hypoallergenic egg?

Liang

Xing

et al. 2020

Journal of Food Science

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Section: Resultsmentioning

confidence: 99%

“…When assessing the digestibility of the ovalbumin with human digestive fluids, Benedé et al [34] reported a lower IgE-binding ability of the resulting peptides. Moreover, Matsuda et al [35] indicated the ability of pepsin to hydrolyse the ovomucoid into three major peptides with a MW of 25kDa, 18kDa and 13kDa, which endured a remarkable decrease in in vivo allergenicity. The allergenicity of egg proteins was generally related to their heat stability, their resistance to enzymatic digestion and the exposure of the existent IgE-binding epitopes [18].…”

Section: Influence Of Protein Hydrolysis On the Antigenic Properties ...mentioning

confidence: 99%

Advances in Understanding the Antioxidant and Antigenic Properties of Egg-Derived Peptides

Brumă (Călin),

Vasilean,

Grigore-Gurgu

et al. 2024

Molecules

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Pepsin, trypsin and proteinase K were used in the present study to hydrolyse the proteins from whole eggs, yolks or whites, and the resulting hydrolysates were characterised in terms of antioxidant and IgE-binding properties, using a combination of in vitro and in silico methods. Based on the degree of hydrolysis (DH) results, the egg yolk proteins are better substrates for all the tested enzymes (DH of 6.2–20.1%) compared to those from egg whites (DH of 2.0–4.4%). The SDS-PAGE analysis indicated that pepsin and proteinase K were more efficient compared to trypsin in breaking the intramolecular peptide bonds of the high molecular weight egg proteins. For all the tested substrates, enzyme-assisted hydrolysis resulted in a significant increase in antioxidant activity, suggesting that many bioactive peptides are encrypted in inactive forms in the parent proteins. The hydrolysates obtained with proteinase K exhibited the highest DPPH radical scavenging activity (124–311 µM Trolox/g protein) and the lowest residual IgE-binding capacity. The bioinformatics tools revealed that proteinase K is able to break the integrity of the main linear IgE-binding epitopes from ovalbumin and ovomucoid. It can be concluded that proteinase K is a promising tool for modulating the intrinsic properties of egg proteins.

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Reduction of Ovomucoid Immunogenic Activity on Peptic Fragmentation and Heat Denaturation

Cited by 2 publications

References 5 publications

Can food processing produce hypoallergenic egg?

Can food processing produce hypoallergenic egg?

Advances in Understanding the Antioxidant and Antigenic Properties of Egg-Derived Peptides

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