Effect of Maillard Reaction on Allergenicity of Scallop Tropomyosin

Nakamura, Atsushi; Watanabe, Kazuhiko; Ojima, Takao; Ahn, Dong-Hyun; Saeki, Hiroki

doi:10.1021/jf0502045

Cited by 113 publications

(88 citation statements)

References 22 publications

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“…However, some studies have demonstrated modulation oflgE recognition to tropomyosin due to heat-induced Maillard reaction, which may occur in some shellfish species (Nakamura et al 2005(Nakamura et al , 2006 According to the AllFam database, the TM f a mily is the largest "food" aller gen f a mily in animal sources, consisting of currently 47 identified TMs, mostly from crustacean species (Radauer et al 2008). Examples of well-characterized TM are Pen m 1, Pen a 1, Lit v 1, and Hom a 1.…”

Section: Structure and Biological Functions Of Shellfish Allergensmentioning

confidence: 99%

Allergens and Molecular Diagnostics of Shellfish Allergy

Lopata

Kleine-Tebbe²,

Kamath

2017

Molecular Allergy Diagnostics

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Section: Structure and Biological Functions Of Shellfish Allergensmentioning

confidence: 99%

Allergens and Molecular Diagnostics of Shellfish Allergy

Lopata

Kleine-Tebbe²,

Kamath

2017

Molecular Allergy Diagnostics

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“…However, these observations may be complicated by the fact that peanut allergens leach out of peanuts during boiling, lowering the residual allergen content in the boiled nuts (Mondoulet et al, 2005). Maillard modification has also been found to increase the IgE-binding capacity of the allergenic shellfish tropomyosin (Nakamura et al, 2005). Individuals may have become sensitised to glycated tropomyosin itself, through consumption of the dried fish products frequently used, especially in oriental cuisine.…”

Section: Processing Induced Chemical Modification Of Allergensmentioning

confidence: 99%

Impact of food processing on the structural and allergenic properties of food allergens

Mills¹,

Sancho

Rigby

et al. 2009

Molecular Nutrition Food Res

192

151

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IntroductionTwo of the major unanswered questions in food allergy research are what makes one person, and not another, become allergic and what are the attributes of some foods and food proteins that make them more allergenic than others? Seeking to answer these questions is much more difficult than investigating the allergenic potency of inhalant or contact allergens since the proteins involved in sensitising or elicting allergic reactions may have undergone extensive modification during food processing and be presented within complex structures within food.These physicochemical changes will alter the way in which they are broken down during digestion and may modify the form in which they are taken up across the gut mucosal barrier and presented to the immune system. Certainly the structure of the food matrix can have a great impact on the elicitation of allergic reactions and fat-rich matrices may affect the kinetics of allergen release, potentiating the severity of allergic reactions (Grimshaw et al., 2003). However, because of its complex nature the impact of food processing and the food matrix on allergenicity of proteins has only recently become a subject of research. Such investigations are fraught with difficulties, not least the fact that food processing often renders food proteins insoluble in the simple salt solutions frequently employed in serological or clinical studies. As a consequence our understanding of the impact of food processing on allergenicity is limited to the more soluble and extractable residues in foods and the allergenic potential of insoluble protein complexes is virtually unstudied despite representing the vast bulk of food proteins consumed. Proteins in fabricated food structuresMuch of our understanding of the effects of food processing on food protein structure and the fabrication of different types of food structure has been gained from studying model food,

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“…Effects of sugar-protein or Maillard reaction on the allergenic property or IgE binding to allergens from shrimp [18], milk [19], buckwheat [20] and peanuts [11][12][13] have been studied. In the latter three studies (peanuts), increased IgE binding has been reported.…”

Section: Ige Binding Of Ribose-treated Peanut Extracts In Elisamentioning

confidence: 99%