Effect of Covalent Interaction with Chlorogenic Acid on the Allergenic Capacity of Ovalbumin

Lu, Yuqin; Li, Shuiming; Xu, Haoxie; Zhang, Tingting; Xiao, Lin; Wu, Xuli

doi:10.1021/acs.jafc.8b03410

Cited by 72 publications

(23 citation statements)

References 31 publications

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“…Reduced IgE-binding capacity Yuan et al (2019) Egg white proteins were preheated at 85°C for 30 min, then Alcalase (free or immobilized) was used for hydrolysis at pH 8 at 60°C from 10 to 250 min Reduced IgE-binding capacity Yang, Long et al (2017) Egg white in the presence or absence of egg yolk 2014; Hildebrandt et al (2008) antioxidant activity (Yang, Tu, Wang, Zhang, & Song, 2018). Both interactions with epigallo-catechin 3-gallate and chlorogenic acid reduced IgE-binding capacity of ovalbumin, due to the shielding of the linear IgE epitope (Lu et al, 2018;Ognjenović et al, 2014). Pulsed electric field treatment > 25 kV/cm (for 180 µs) or at 35 kV/cm for long time (>60 µs) was proven to reduce the IgE binding of ovalbumin, due to aggregate formation (Yang, Zhang et al, 2017).…”

Section: Processing Condition Allergenicity Change Referencesmentioning

confidence: 99%

“…However, ultrasound combined with glycation has been reported to be effective in reducing its IgE‐binding ability as well as enhancing its antioxidant activity (Yang, Tu, Wang, Zhang, & Song, 2018). Both interactions with epigallo‐catechin 3‐gallate and chlorogenic acid reduced IgE‐binding capacity of ovalbumin, due to the shielding of the linear IgE epitope (Lu et al., 2018; Ognjenović et al., 2014). Pulsed electric field treatment > 25 kV/cm (for 180 µs) or at 35 kV/cm for long time (>60 µs) was proven to reduce the IgE binding of ovalbumin, due to aggregate formation (Yang, Zhang et al., 2017).…”

Section: Effect Of Processing On Allergenicity Of Eggmentioning

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: Effect Of Processing On Allergenicity Of Eggmentioning

confidence: 99%

Can food processing produce hypoallergenic egg?

Liang

Xing

et al. 2020

Journal of Food Science

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“…Stanic-Vucinic et al (2013) reported that chemical modification of β-LG is associated with structural and functional modification of proteins, which in turn may increase their allergenic potential by exposing hidden epitopes or creating new epitopes [78]. While the reaction of β-LG with lactose in milk showed increased allergenic activity [79], the allergenicity could be reduced by the covalent modification of ovalbumin [80] and the whey protein β-LG [7,81] with polyphenols in vitro.…”

Section: Discussionmentioning

confidence: 99%

Immunological Analysis of Isothiocyanate-Modified α-Lactalbumin Using High-Performance Thin Layer Chromatography

et al. 2021

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Undirected modifications between food proteins and secondary plant metabolites can occur during food processing. The results of covalent interactions can alter the functional and biological properties of the proteins. The present work studied the extent of which covalent conjugation of the bioactive metabolite benzyl isothiocyanate (BITC; a glucosinolate breakdown product) to the whey protein α-lactalbumin affects the protein’s allergenicity. Additional to the immunological analysis of native untreated and BITC-modified α-lactalbumin, the analysis of antigenic properties of proteolytically digested protein derivatives was also performed by high performance thin layer chromatography and immunostaining. As a result of the chemical modifications, structural changes in the protein molecule affected the allergenic properties. In this process, epitopes are destroyed or inactivated, but at the same time, buried epitopes can be exposed or newly formed, so that the net effect was an increase in allergenicity, in this case. Results from the tryptic hydrolysis suggest that BITC conjugation sterically hindered the cleavage sites for the enzyme, resulting in reduced digestibility and allergenicity. Residual antigenicity can be still present as short peptide fragments that provide epitopes. The desire to make food safer for allergy sufferers and to protect sensitized individuals from an allergenic reaction makes it clear that the detection of food antigens is mandatory; especially by considering protein interactions.

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“…This screening, in concert with further in vitro experiments revealed that procyanidin C1 and chlorogenic acid could potentially interact with Ara h 2 inducing conformational changes, which masked the IgE epitope [45]. Covalent interactions between chlorogenic acid and ovalbumin (OVA), the major allergen found in the egg white, also induced modifications in OVA conformation, resulting in the direct shielding of the linear IgE epitope, which attenuated allergic mechanisms [46]. Accordingly, histamine release experiments, showed that the basophil degranulation was inferior in human basophils sensitized with the OVA conjugated with chlorogenic acid when compared to OVA unconjugated, implying a decrease in the crosslinking of the FcεRI receptors via IgEallergen interaction [46].…”

Section: Food Allergiesmentioning

confidence: 94%

“…Covalent interactions between chlorogenic acid and ovalbumin (OVA), the major allergen found in the egg white, also induced modifications in OVA conformation, resulting in the direct shielding of the linear IgE epitope, which attenuated allergic mechanisms [46]. Accordingly, histamine release experiments, showed that the basophil degranulation was inferior in human basophils sensitized with the OVA conjugated with chlorogenic acid when compared to OVA unconjugated, implying a decrease in the crosslinking of the FcεRI receptors via IgEallergen interaction [46]. Also, the ability of phenolic compounds to bind to dietary allergen is pointed out as having a beneficial effect due to precipitation events [47].…”

Section: Food Allergiesmentioning

confidence: 99%

Eat Tasty and Healthy: Role of Polyphenols in Functional Foods

Bessa-Pereira¹,

Dias²,

Brandão³

et al. 2021

Functional Foods - Phytochemicals and Health Promoting Potential

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Adverse reactions to food such as allergies and celiac disease are increasingly recognized as a growing public health burden. There is currently no cure for these diseases so that there is an unmet need to evaluate different nutritional approaches aiming at improving the quality of life of affected patients and their families. In this context, healthy promising nature-derived compounds, most of which contained in fruits and vegetables, have been studied as an alternative to attenuate the epidemic. Indeed, phenolic compounds have become an emerging field of interest in nutrition in the last decades. A growing build of research suggests that phenolic compounds inhibit pro-inflammatory transcription factors by interacting with proteins involved in gene expression and cell signaling, leading to protective effects against many inflammation-mediated chronic diseases. However, the use of phenolic compounds as attenuating agents of immune reactions to food has to be aligned to the organoleptic characteristics of food, since many compounds present unpleasant taste properties, namely bitter taste and astringency. In this framework, tasty but healthy phenolic compounds arise as attractive ingredients in the design and formulation of functional foods. This book chapter is focused on revisiting the organoleptic properties of phenolic compounds while evaluating the role of these compounds in health promoting actions, namely the management of immune reactions to food such as Food Allergies and Celiac Disease.

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Effect of Covalent Interaction with Chlorogenic Acid on the Allergenic Capacity of Ovalbumin

Cited by 72 publications

References 31 publications

Can food processing produce hypoallergenic egg?

Can food processing produce hypoallergenic egg?

Immunological Analysis of Isothiocyanate-Modified α-Lactalbumin Using High-Performance Thin Layer Chromatography

Eat Tasty and Healthy: Role of Polyphenols in Functional Foods

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