Quantification of allergenic plant traces in baked products by targeted proteomics using isotope marked peptides

Huschek, Gerd; Bönick, Josephine; Löwenstein, Yvonne; Sievers, Steven; Rawel, Harshadrai M.

doi:10.1016/j.lwt.2016.07.057

Cited by 28 publications

(14 citation statements)

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“…Three peptides (8–18 amino acids) for each legume species were finally chosen as peptide markers from the group of the candidate marker peptides due to their highest intensities in spiked sausages (test sausage T4, see Table 1 ) applying the optimized MRM method (see Section 3.2 .). The final selected peptides QQEQQLEGELEK [ 25 ], NTLEATFNTR [ 25 , 31 ], and ISSVNSLTLPILR [ 25 ] for lupine blue, NPYHFSSQR [ 31 ] for lupine white, ELTFPGSVQEINR, LSSGDVFVIPAGHPVAVK, and LTPGDVFVIPAGHPVAVR for pea [ 25 ], GTGNLELVAVR [ 32 , 33 , 34 , 35 , 36 ], FNLAGNHEQEFLR [ 32 , 33 , 37 , 38 ], and WLGLSAEYGNLYR [ 32 , 34 ] for peanut, and SQSDNFEYVSFK [ 23 , 34 , 36 ], EAFGVNMQIVR [ 25 , 34 , 38 , 39 ], and FYLAGNQEQEFLK [ 22 , 23 , 25 , 36 ] for soy have been reported previously in the scientific literature. The identities of each of the 14 marker peptides for alfalfa, broad bean, chickpea, and lentil, as well as lupine white 2 and 3, which have not been reported in the literature until now, were confirmed by spiking in a tryptic digest of an emulsion-type sausage (test sausage T4).…”

Section: Resultsmentioning

confidence: 99%

A UHPLC-MS/MS Method for the Detection of Meat Substitution by Nine Legume Species in Emulsion-Type Sausages

Spörl

Speer²,

Jira

2021

Foods

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Meat substitution by legume proteins in various types of meat products is a common practice. A reliable detection and quantification of these additives is required to control food specifications, especially regarding food fraud. Consequently, a UHPLC-MS/MS method for the simultaneous detection of alfalfa (Medicago sativa), broad bean (Vicia faba), chickpea (Cicer arietinum), lentil (Lens culinaris), lupine (Lupinus albus and Lupinus angustifolius), pea (Pisum sativum), peanut (Arachis hypogaea), and soy (Glycine max) proteins in meat products was developed. After protein extraction and tryptic digestion, three marker peptides for each legume species were measured by multiple reaction monitoring (MRM) using an optimized extraction protocol. To the best of our knowledge, the marker peptides for alfalfa, broad bean, chickpea, and lentil have not been reported previously. Emulsion-type sausages with 0.1, 0.4, 0.7, 1.0, 1.3, 1.6, 1.9, 2.2, and 2.5% meat substitution by each legume species, representing the concentration range between inadvertently transferred cross-contaminations and the conscious use for meat substitution, were produced for matrix calibration. No false-positive results were recorded in blank samples. In the quantification of alfalfa, broad bean, chickpea, lentil, pea, peanut, and soy, 673 of 756 measuring data of the recovery rate in unknown sausages were in the accepted range of 80–120%.

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Section: Resultsmentioning

confidence: 99%

A UHPLC-MS/MS Method for the Detection of Meat Substitution by Nine Legume Species in Emulsion-Type Sausages

Spörl

Speer²,

Jira

2021

Foods

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“…The method reached a sensitivity down to 2.0 mg/kg of lupine protein in sausages using a peptide marker for β‐conglutin from L. angustifolius , being comparable to those of PCR or ELISA, which ranged between 1 mg/kg (Holden et al., 2005; Holden et al., 2007; Kaw et al., 2008) and 10 mg/kg (Ecker, Ertl, Pulverer, et al., 2013; Waiblinger, Boernsen, Naumann, & Koeppel, 2014). Similarly, other works using HPLC–MS/MS and UPLC–MS/MS reported sensitivities between 0.05 and 24.0 mg/kg in pasta, cookies, and beverages (Huschek, Bonick, Lowenstein, Sievers, & Rawel, 2016; Locati, Morandi, Zanotti, & Arnoldi, 2006; Mane, Bringans, Johnson, Pareek, & Utikar, 2017; Mattarozzi, Bignardi, Elviri, & Careri, 2012; Resta, Brambilla, & Arnoldi, 2012). It is also important to highlight that MS‐based methods go beyond the detection/quantification of lupine, allowing to further confirm its species identity, representing an additional advantage over the immunoassays.…”

Section: Analytical Methods For Lupine Detection In Foodsmentioning

confidence: 63%

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

Villa

Costa

2020

Comp Rev Food Sci Food Safe

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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]).

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“…Furthermore, it was deduced that Sui p 2 is a thermostable protein. Hence, these deduced conformational epitopes will be preserved even if it is exposed in the harsh environment outside the source organism (Vanga et al, 2018;Huschek et al, 2016;Pfeifer et al, 2015). Also, it was reported that subjecting a thermostable allergen to heat treatment can increase its IgE binding affinity due to the slight change in its conformation, which grants better accessibility to otherwise hidden epitopes (Pfeifer et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

cDNA Cloning and Characterization of the House Dust Mite Allergen Sui p 2

Bajao¹,

Ramos²

2020

American Journal of Biochemistry and Biotechnology

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Suidasia pontifica (Sp) is a House Dust Mite (HDM) species found in tropical urban residential areas which causes sensitization of up to 75% of allergic patients. Cloning of allergens from Sp is a significant initial step in understanding the clinical significance of this HDM species. The study describes the cloning and in silico characterization of the group 2 allergen gene from Sp (Sui p 2) with significant homology to Myeloid Differentiation 2 (MD-2) lipid-binding (ML domain) protein allergens. Sui p 2 gene was amplified by Reverse Transcription-PCR using gene-specific primers designed from known HDM group 2 allergens. The amplicons were characterized using NCBI BLAST, ExPASy, MEGA7 and Chimera. Sui p 2 cDNA gene exhibits percent identity to Tyrophagus putrescentiae (65.84%), Aleuroglyphus ovatus (65.69%) and Blomia tropicalis (62.98%). Sui p 2 gene contains 405 bp open reading frame with untranslated regions on its 5' and 3' end. Furthermore, structure-based percent identity of Sui p 2 to the group 2 allergen of D. farinae and D. pteronyssinus is 47.62% and 46.83%, respectively. Predicted protein structure reveals a putative immunoglobulin fold consisting of preserved cysteine residues, hydrophobic core and two antiparallel β-sheets containing several TLR4, LPS and IgE binding sites. The results suggest that Sui p 2 may play an important role in HDM induced allergy and may be involved in the induction of the innate immune system. Characterization of Sui p 2 is important to evaluate properly its use for allergy component resolved diagnosis and allergen-specific immunotherapy.

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Quantification of allergenic plant traces in baked products by targeted proteomics using isotope marked peptides

Cited by 28 publications

References 30 publications

A UHPLC-MS/MS Method for the Detection of Meat Substitution by Nine Legume Species in Emulsion-Type Sausages

A UHPLC-MS/MS Method for the Detection of Meat Substitution by Nine Legume Species in Emulsion-Type Sausages

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

cDNA Cloning and Characterization of the House Dust Mite Allergen Sui p 2

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