Effect of heat treatment on milk and egg proteins allergenicity

Bloom, K.A.; Huang, Faith; Bencharitiwong, Ramon; Bardina, L.; Ross, Andrew; Sampson, Hugh A.; Nowak‐Węgrzyn, Anna

doi:10.1111/pai.12283

Cited by 162 publications

(123 citation statements)

References 24 publications

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“…Heat causes protein denaturation and aggregation during temperature changes from 60 to 90°C, which may cause that high molecular mass peptides form clusters and, as a result, may hinder binding ability of the enzyme. Thus, bioactivity may diminish or be lost (Bloom et al 2015). In agreement with research by Wu et al (2014), this work suggested that hydrolysates with ACEIA could be stable in the heat and time treatments of food processes carried out in temperatures ranging from 60 to 100°C and also for short periods of time.…”

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confidence: 72%

Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain

et al. 2016

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The aim of this work was to assess the effects of temperature (T), time (t) and pH treatments and an in vitro digestion on the stability of the angiotensin I-convertingenzyme-inhibitory activity (ACEIA) and antithrombotic activity (ATA; assessed as inhibition of platelet aggregation) of selected protein hydrolysates of amaranth named Alb1H103 and GloH88 and GluH24 with dipeptidyl peptidase IV inhibitory activity (DPPIVIA). Heat treatment (40-100°C) for 1 h showed no significant differences among ACEIA, DPPIVIA and ATA of the heated hydrolysates at pH 4 and 7. There was no statistically significant loss of any bioactivity under heat treatment for 3 h at pH 4.0. Alb1H103 and GluH24 maintained the inhibitory activity of ACE and ATA at pH 7.0 for 3 h, whereas GloH88 maintained ACEIA and ATA for 2.0 h at pH 7.0. The pH effect on hydrolysates bioactivity was assessed in the range of 2.0-12.0. This was negligible on ACEIA, ATA and DPPIVIA. The in vitro digestion was performed using pepsin, trypsin (T) and a-chymotrypsin (C). A previous treatment of hydrolysates with pepsin improved the proteolytic activities of T and C. The hydrolysates kept at 100°C for 1 h at pH 4.0, showed a significant increase in bioactivity. Conversely, a treatment at pH 7.0 showed no significant difference (p \ 0.05) in the hydrolysates bioactivities after their digestion. Thus, biological activity of hydrolysates may be preserved or enhanced, depending on their processing conditions.

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supporting

confidence: 72%

Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain

et al. 2016

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“…Allergic potency of egg in particular vastly changes by cooking or processing because heating reduces or denatures allergen epitopes 25. For this reason, we estimated the ability of EW‐ and OM‐sIgEs to predict a positive response when a patient is exposed to either cooked or raw egg in an OFC.…”

Section: Discussionmentioning

confidence: 99%

Predictive values of egg‐specific IgE by two commonly used assay systems for the diagnosis of egg allergy in young children: a prospective multicenter study

Furuya

Nagao

Sato

et al. 2016

Allergy

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BackgroundSpecific IgE (sIgE) is often used to predict oral food challenge (OFC) outcomes in food allergy, but interpretation of the results may vary depending on the assay method employed and the patient population tested. The aim of this study was to use two commercial assay systems to determine egg‐sIgE values predictive of allergy within the most common populations treated at pediatric clinics.MethodsIn a multicenter prospective study, 433 children with suspected or confirmed egg allergy underwent oral challenge (OFC) using cooked egg (CE) and raw egg (RE) powders to diagnose either true allergy in 1‐year‐old (group A, n = 220) or tolerance in 2‐ to 6‐year‐old (group B, n = 213). Egg white (EW)‐ and ovomucoid (OM)‐sIgE values were measured using the ImmunoCAP ® sIgE (ImmunoCAP) and the IMMULITE ® 2000 3 gAllergy™ (3gAllergy) systems. Children were recruited from six primary care clinics and 18 hospitals in Japan.ResultsReceiver‐operating characteristic (ROC) curve analysis yielded similar areas under the curve (AUC) for the two assays (0.7–0.8). The optimal cutoff values and the probability curves (PCs) of the sIgE by the two assays to predict CE and RE OFC outcomes were determined for both groups. Values for 3gAllergy were higher than for ImmunoCAP; however, correlation of sIgE and predicted probability calculated by PCs were strong between the two methods.ConclusionsCutoff values and PCs for egg‐sIgE established using both ImmunoCAP and 3gAllergy may be useful for predicting egg allergy in early childhood patient populations.

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“…Roasting increases the allergenicity of peanuts compared to boiling or pickling whereas heating of cow's milk and hen's egg reduces their allergenicity such that 50-75 % of allergic children tolerate them in baked products [31][32][33]. A wheat matrix together with milk or egg resulted in decreased IgE antibody binding to milk and egg white proteins amongst milk-and egg-allergic children.…”

Section: The Degree Of Processing or Matrix Used To Disguise A Food Amentioning

confidence: 94%

“…A wheat matrix together with milk or egg resulted in decreased IgE antibody binding to milk and egg white proteins amongst milk-and egg-allergic children. The authors suggest this is due to the formation of complexes between wheat and milk protein/egg proteins which reduces the bioavailability of milk/egg protein to the immune system [33]. Wheat matrix effects for other allergens have not been described but if present could result in higher eliciting doses.…”

Section: The Degree Of Processing or Matrix Used To Disguise A Food Amentioning

confidence: 97%

Oral Food Challenges: The Design must Reflect the Clinical Question

Feeney

Marrs

Lack

et al. 2015

Curr Allergy Asthma Rep

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Oral food challenges are the gold-standard diagnostic investigation for diagnosing food allergy. They allow a subject to consume an age-appropriate portion of allergenic food under surveillance to assess whether a reproducible immune-mediated adverse response is demonstrated. The specific design of food challenge must closely reflect the anticipated management step being considered. In clinical practice, food challenges are most commonly used to investigate the subject's status of allergy or tolerance to a food. However, other characteristics of food allergy are increasingly being investigated through recent studies. In particular, studies investigating food allergy prevention strategies, the impact of oral immunotherapy on subjects' threshold for allergic reactions and also their potential acquisition of long-term tolerance each utilize differing designs of oral food challenges to investigate their specific hypothesis. We examine how oral food challenges may be designed to assess specific characteristics of the food allergic response.

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Effect of heat treatment on milk and egg proteins allergenicity

Abstract: Heating has a different effect on whey and caseins in cow's milk and ovalbumin and ovomucoid in hen's egg white. The effect of heat on protein allergenicity is affected by the temperature and duration, along with the presence of wheat.

Cited by 162 publications

References 24 publications

Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain

Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain

Predictive values of egg‐specific IgE by two commonly used assay systems for the diagnosis of egg allergy in young children: a prospective multicenter study

Oral Food Challenges: The Design must Reflect the Clinical Question

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