Contribution of Structural Reversibility to the Heat Stability of the Tropomyosin Shrimp Allergen

Usui, Masakatsu; Harada, Akihito; Ishimaru, Takayuki; Sakumichi, Emiri; Saratani, Fumihiko; Sato-Minami, Chiho; Azakami, Hiroyuki; Miyasaki, Taiko; Hanaoka, Ken’ichi

doi:10.1271/bbb.120887

Cited by 35 publications

(15 citation statements)

References 17 publications

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“…Another possibility is the formation of soluble aggregates, which was also demonstrated for the Japanese cedar pollen allergen Cry j 1 by Aoki et al [23]. Moreover, Usui et al [24] showed that heat processing of purified tropomyosin from shrimp did not induce the formation of insoluble aggregates. However, difference in solubility in PBS buffer between heated and unheated tropomyosin was not in agreement with our results.…”

Section: Discussionmentioning

confidence: 86%

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Effect of thermal processing on mealworm allergenicity

Broekman

Knulst

Jäger

et al. 2015

Molecular Nutrition Food Res

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Section: Discussionmentioning

confidence: 86%

“…Moreover, Usui et al. showed that heat processing of purified tropomyosin from shrimp did not induce the formation of insoluble aggregates. However, difference in solubility in PBS buffer between heated and unheated tropomyosin was not in agreement with our results.…”

Section: Discussionmentioning

confidence: 99%

Effect of thermal processing on mealworm allergenicity

Broekman

Knulst

Jäger

et al. 2015

Molecular Nutrition Food Res

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“…Crustacean tropomyosin re-folds after heating (Usui et al, 2013) and is heat resistant (Shanti et al, 1993;Leung et al, 1994;Crespo et al, 1995b;Samson et al, 2004). Whereas tropomyosin increases its IgE-binding capacity after boiling (Liu AH et al, 2010;Shriver et al, 2011;Kamath et al, 2013), extracts from boiled shrimp showed reduced IgE-binding, which points to a role of other heat-sensitive allergens in IgE-binding to the extract.…”

Section: Heat Treatmentmentioning

confidence: 99%

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2014

EFSA Journal

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Following a request from the Food Safety Authority of Ireland, the EFSA Panel on Dietetic Products, Nutrition and Allergies (NDA Panel) was asked to deliver a scientific opinion on the evaluation of allergenic foods and food ingredients for labelling purposes. In view of the request, the NDA Panel decided to update its previous opinions relative to food ingredients or substances with known allergenic potential listed in Annex IIIa of 2003/89/EC, as amended. These include cereals containing gluten, milk and dairy products, eggs, nuts, peanuts, soy, fish, crustaceans, molluscs, celery, lupin, sesame, mustard and sulphites. The opinion relates to immunoglobulin (Ig)E-and non-IgE-mediated food allergy, to coeliac disease and to adverse reactions to sulphites in food, and it does not address non-immune-mediated adverse reactions to food. It includes information on the prevalence of food allergy in unselected populations, proteins identified as food allergens, cross-reactivities, the effects of food processing on the allergenicity of foods and ingredients, methods for the detection of allergens and allergenic foods, doses observed to trigger adverse reactions in sensitive individuals and risk assessment methodologies that have been used to derive individual and population thresholds for selected allergenic foods. The present opinion relates to immunoglobulin (Ig)E-and non-IgE-mediated food allergy, to coeliac disease and to adverse reactions to sulphites in food, and it does not address non-immune-mediated adverse reactions to food. For each food ingredient or substance listed in Annex IIIa, it includes information on the prevalence of food allergy in unselected populations, on proteins identified as food allergens, on cross-reactivities, on the effects of food processing on the allergenicity of foods and ingredients, on methods for the detection of allergens and allergenic foods, and on doses observed to trigger adverse reactions in sensitive individuals.Immune-mediated adverse reactions to foods manifest with clinical signs and symptoms of variable severity and duration, which may affect different organs and systems. Anaphylactic reactions to food are IgE mediated and may occur at any age. Non-IgE-mediated food allergy includes a wide range of diseases, including protein-induced enterocolitis and eosinophilic oesophagitis.A careful family and clinical history are the basis for diagnosis of food allergy. Food diaries, skin prick tests (SPTs), allergen-specific IgE measurements, food elimination diets and food challenges are part of the standard protocol for the diagnosis of food allergy. A positive SPT indicates sensitisation to the tested food, but it is not diagnostic of food allergy. Allergen-specific serum IgE antibodies similarly denote sensitisation to a particular food, but they are not diagnostic without a clinical history or food challenge. The use of atopy patch tests for the diagnosis of food allergy is controversial. Other available tests have no current role in the diagnosis of food allergy. Diag...

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“…4,5) In a previous study, we reported that tropomyosin is heat-stable even at high temperatures. 6) However, the properties of the isolated allergen present in food do not necessarily reflect the overall risk of allergy. Thus, we investigated the effects of tropomyosin concentrations from cooked or raw shrimp and those with varying levels of freshness because of different storage conditions to better understand the allergy risk of eating shrimp.…”

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confidence: 99%

“…Furthermore, the hydrophilic amino acid-rich sequence and absence of cysteine residues contributed to the solubility of shrimp tropomyosin at high temperatures. 6) In addition to these properties, because tropomyosin did not covalently bind with the protein-formed muscle fibril, nonphysiological muscle contraction-involved fibril protein denaturation by heat stress may facilitate the disassociation and elution of tropomyosin to PBS. Heat stability of tropomyosin and denaturation of other proteins caused by cooking were closely related to a high extraction efficiency.…”

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confidence: 99%

Relationship between the risk for a shrimp allergy and freshness or cooking

Usui

Harada

Yasumoto

et al. 2015

Bioscience, Biotechnology, and Biochemistry

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Tropomyosins are defined as risk factors for shrimp allergy. However, their concentration in different preparations has not been clarified. We quantified the tropomyosin concentration in shrimp meat, which was cooked using several methods or was stored under various conditions. The results demonstrated that shrimp meat from various preparations and storage conditions maintained tropomyosin concentrations that were sufficient to cause food allergies.

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Contribution of Structural Reversibility to the Heat Stability of the Tropomyosin Shrimp Allergen

Cited by 35 publications

References 17 publications

Effect of thermal processing on mealworm allergenicity

Effect of thermal processing on mealworm allergenicity

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Relationship between the risk for a shrimp allergy and freshness or cooking

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