Lupin Allergen Detection

Fæste, Christiane Kruse

doi:10.1002/9780470637685.ch22

Cited by 2 publications

(9 citation statements)

References 96 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Among sensitized children, 6% were diagnosed with soybean allergy while an overall prevalence of 2.1% was found in a study involving several European countries, the USA, and Australia [1,4,5]. Regarding lupine allergy, the prevalence varies, depending on dietary habits and geographical differences [1,6].…”

Section: Introductionmentioning

confidence: 99%

Immunoreactivity of Lupine and Soybean Allergens in Foods as Affected by Thermal Processing

Villa

Moura

Costa

2020

Foods

View full text Add to dashboard Cite

Lupine and soybean are important technological aids for the food industry. However, they are also capable of inducing severe allergic reactions in food-sensitized/allergic individuals. In this context, this work intended to study the combined effects of thermal processing and food matrix on the immunoreactivity of lupine and soybean proteins used as ingredients in bakery and meat products, respectively. For this purpose, the effects of baking, mild oven cooking, and autoclaving on the protein profiles were evaluated, using model mixtures simulating the production of lupine-containing breads and soybean-containing cooked hams/sausages, by native- and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and immunoblotting using specific antibodies. The results showed that lupine gamma-conglutin immunoreactivity was slightly decreased in wheat flour mixtures compared to rice, but it was more pronounced in baked products. In meat mixtures, substantial protein fragmentation was noted after autoclaving, with decreased immunoreactivity of soybean trypsin inhibitor. The analysis of 22 commercial products enabled the identification of lupine gamma-conglutin in four bakery samples and soybean trypsin-inhibitor in five sausages, and further differentiated autoclaved from other milder thermally treated products. Generally, the immunoreactivity of target proteins was reduced by all the tested thermal treatments, though at a higher extent after autoclaving, being slightly altered by the food matrix.

show abstract

Section: Introductionmentioning

confidence: 99%

Immunoreactivity of Lupine and Soybean Allergens in Foods as Affected by Thermal Processing

Villa

Moura

Costa

2020

Foods

View full text Add to dashboard Cite

show abstract

“…The prevalence of lupine sensitization is unknown, depending on the dietary habits and geographical differences, although it has been reported to grow in parallel with its increasing consumption (Faeste, 2010;Verma et al, 2013). A study developed by Reis et al (2007), using data of 1,160 individuals from the Mediterranean region (Portugal) with suspicion of food allergy, reported 4.1% of lupine sensitization confirmed by skin prick tests (SPT) among the test population.…”

Section: Prevalence and Clinical Reactivitymentioning

confidence: 99%

“…Lupine profilin .1 -single-and two-cupin domains, the latter including the 7S (vicilins) and the 11S (legumins) seed storage proteins (Faeste, 2010). β-Conglutin was characterized in 2008 as a major allergen in L. angustifolius (Goggin, Mir, Smith, Stuckey, & Smith, 2008), being added to the allergen list as Lup an 1 (WHO/IUIS [http://www.allergen.org/]).…”

Section: β-Conglutin (Lup a 1 And Lup An 1)mentioning

confidence: 99%

Section: Lupine Allergymentioning

confidence: 99%

“…Another α‐conglutin was also identified in the L. mutabilis , being considerably different, both in composition and structure, from its counterpart in L. albus (Santos, Ferreira, & Teixeira, 1997), but it is not classified as an allergenic protein, most likely because this species is not frequently consumed and, consequently, not extensively studied. In L. albus , α‐conglutin is an oligomeric protein consisting of hexamers of disulfide‐linked basic and glycosylated acidic trimers (typical structure of legumins), constituted by four subunits of 50 to 60 kDa (Carvajal‐Larenas et al., 2016; Duranti et al., 2008; Fæste, 2010). In immature subunits, the predominant form of the protein is a trimer (Adachi et al., 2003), but after pro‐polypeptide cleavage, the mature subunits are divided into acidic (heavier) (38 to 54 kDa) and basic (lighter) (19 to 22 kDa) polypeptide chains (Duranti et al., 2008; Santos et al., 1997).…”

Section: Molecular Characterization Of Lupine Allergensmentioning

confidence: 99%

See 2 more Smart Citations

Lupine allergens: Clinical relevance, molecular characterization, cross‐reactivity, and detection strategies

Villa

Costa

2020

Comp Rev Food Sci Food Safe

View full text Add to dashboard Cite

Lupine is commonly utilized as a technological food and ingredient in a great variety of processed products (snacks, bakery, meat, and dairy products) principally owing to its nutritional value and technological properties. However, its ingestion, even at trace amounts (in the range of mg protein per kg of food), can lead to severe adverse reactions in allergic individuals. Lupine belongs to the Leguminosae family, having the conglutins (α-, β-, δ-, and γ-) as allergens, among other proteins. Cross-sensitization of lupine-sensitized individuals with other legume species, mainly peanut, can occur, but the associated clinical reactivity is still unclear. The protection of the sensitized individuals should depend on an avoidance diet, which should rely on the compliance of food labeling and, as such, on their verification by analytical methods. Food processing, such as heat treatments, has an important influence on the structural properties of lupine proteins, altering their detectability and allergenicity. In this review, different aspects related with lupine allergy are described, namely, the overall prevalence, clinical relevance, diagnosis, and treatment. The characterization of lupine allergens and their potential cross-reactivity with other legumes are critically discussed. The effects of food matrix, processing, and digestibility on lupine proteins, as well as the available analytical tools for detecting lupine at trace levels in foods, are also herein emphasized. K E Y W O R D S allergen, analytical methods, food allergy, Lupinus species, protein 1 INTRODUCTION Lupine belongs to the Lupinus genus from the Fabaceae or Leguminosae family, which also comprises soybean, peanut, chickpea, and other types of legumes (Villarino, Jayasena, Coorey, Chakrabarti-Bell, & Johnson, 2016). From approximately 450 known species of lupine, four are of agricultural and commercial interest: Lupinus albus (white lupine), native from the Mediterranean region and Africa; Lupinus angustifolius (blue lupine) from Australia; Lupinus luteus (yellow lupine) from Central Europe; and Lupinus mutabilis from South America (Jappe & Vieths, 2010; Sanz, de Las Marinas, Fernandez, & Gamboa, 2010). According to FAOSTAT, a total world production of 1,188,213 tonnes of lupine was reached in 2018. Australia is the main producer, with 714,254 tonnes in 2018, accounting to 60.1% of total world lupine production. In Europe, Russia and Poland are the main producers, reaching 136,352 and 124,314 tonnes in 2018, respectively, corresponding to 39.9% and 36.4% of total lupine production in Europe, respectively (FAOSTAT [http://www.fao.org/ faostat/en/#home]).

show abstract

Lupin Allergen Detection

Cited by 2 publications

References 96 publications

Immunoreactivity of Lupine and Soybean Allergens in Foods as Affected by Thermal Processing

Immunoreactivity of Lupine and Soybean Allergens in Foods as Affected by Thermal Processing

Lupine allergens: Clinical relevance, molecular characterization, cross‐reactivity, and detection strategies

Contact Info

Product

Resources

About