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1.
The functionality of light roasted peanut flour (PF) dispersions containing supplemental casein (CN) was altered after polymerization with microbial transglutaminase (TGase). The formation of high molecular weight covalent cross-links was observed with likely development of PF-PF, PF-CN, and CN-CN polymers based on Western blotting patterns visualized using antiserum directed against Ara h 1, Ara h 2, Ara h 3, or casein. The gelling temperature of TGase-treated PF dispersions containing 2.5% CN was significantly raised compared to the nontreated PF-CN control solutions. Furthermore, the gel strength and water holding capacity of cross-linked PF-CN test samples containing 5% CN was increased, while the yield stress and apparent viscosity were lowered compared to control dispersions. The immunological staining patterns were also changed where, in some cases, IgE binding to TGase-treated PF-CN fractions appeared less reactive compared to equivalent polymeric PF dispersions lacking supplemental CN and non-cross-linked PF-CN samples. Perhaps, covalent modification masked IgE peanut protein binding epitopes, at least to some degree, on an individual patient basis. Casein proved to be an effective cosubstrate with PF for creating Tgase modified PF-CN dispersions for use as a novel high protein food ingredient.  相似文献   

2.
Mildly extracted peanut allergen Ara h 1 was previously reported to occur as an oligomeric complex. In this paper we describe how the protein in this oligomeric complex interacts noncovalently with phenolic compounds of the proanthocyanidin type. These interactions are being disrupted during anion exchange chromatography, resulting in the dissociation of the oligomeric Ara h 1 complex into protein trimers. By use of the known three-dimensional structure of beta-conglycinin, a soy protein homologous to Ara h 1, proline-rich regions were observed in silico on both faces of its trimeric structure, which are conserved in Ara h 1. These proline-rich regions could explain the binding of proanthocyanidins to Ara h 1 and the formation of multiple Ara h 1 trimer complexes. This was supported by the observation that the addition of peanut proanthocyanidins to trimeric Ara h 1 and to beta-conglycinin resulted in the formation of soluble oligomeric protein complexes. The structurally related legumin proteins do not contain such proline-rich regions on both sides of the protein, and proanthocyanidins were shown to have a lower affinity for legumin proteins from peanuts and soybeans (peanut allergen Ara h 3 and soy glycinin, respectively). Ara h 1 present as the oligomeric complex is assumed to be the representative form of the allergen in which it is consumed by humans.  相似文献   

3.
Numerous food allergens of plant origin belong to the 2S albumin family, including peanut Ara h 2. In addition to Ara h 2, several other conglutins related to 2S albumins are present in peanut seeds. We evaluated the allergenicity of different peanut conglutins as compared with Ara h 2. Several conglutins were isolated from the kernel, i.e. Ara h 2, a new isoform of Ara h 6 and its derived product, which is likely to be naturally formed during seed processing. Enzyme allergosorbent tests performed on sera of peanut allergic patients showed that more than 94% of 47 analyzed patients had positive IgE responses to Ara h 6 isoform and to its degradation product. Skin prick tests with the new isoform of Ara h 6 led to a positive response in seven out of the eight tested patients. Both enzyme allergosorbent tests and skin prick tests showed that the reactivity of Ara h 6 was similar to, or even higher than, that of Ara h 2, suggesting that the present isoform of Ara h 6 is as allergenic as Ara h 2. In addition the IgE response to the plant processed (i.e., hydrolyzed) Ara h 6 new isoform is equivalent to the IgE response to the native isoform. The IgE immunoreactivity is mostly abrogated by chemical reduction and denaturation of Ara h 6 isoforms, which underlined the importance of tertiary structure in Ara h 6 immunoreactivity. These results, and particularly the high correlation between anti-Ara h 2 and anti-Ara h 6 IgE responses, emphasise the major role of 2S albumins in peanut allergenicity.  相似文献   

4.
Peanut allergy is a public health issue. The culprits are the peanut allergens. Reducing the allergenic properties of these allergens or proteins will be beneficial to allergic individuals. In this study, the objective was to determine if peroxidase (POD), which catalyzes protein cross-linking, reduces the allergenic properties of peanut allergens. In the experiments, protein extracts from raw and roasted defatted peanut meals at pH 8 were incubated with and without POD in the presence of hydrogen peroxide at 37 degrees C for 60 min. The POD-treated and untreated samples were then analyzed by SDS-PAGE, western blots, and competitive inhibition ELISA. IgE binding or allergenicity was determined in blots and ELISA. Results showed that POD treatment had no effect on raw peanuts with respect to protein cross-linking. However, a significant decrease was seen in the levels of the major allergens, Ara h 1 and Ara h 2, in roasted peanuts after POD treatment. Also, polymers were formed. Despite this, a reduction in IgE binding was observed. It was concluded that POD induced the cross-linking of mainly Ara h 1 and Ara h 2 from roasted peanuts and that, due to POD treatment, IgE binding was reduced. The finding indicates that POD can help reduce the allergenic properties of roasted peanut allergens.  相似文献   

5.
Phytic acid would form soluble and insoluble complexes with proteins. Our objective was to determine if phytic acid forms insoluble complexes with major peanut allergens, and if such reaction results in a peanut extract with a lower level of soluble allergens and allergenic property. Extracts from raw and roasted peanuts were treated with and without phytic acid at various pH values and then analyzed by SDS-PAGE and a competitive inhibition ELISA (ciELISA). The ciELISA measured IgE binding using a pooled serum from peanut-allergic individuals. Results showed that phytic acid formed complexes with the major peanut allergens (Ara h 1 and Ara h 2), which were insoluble in acidic and neutral conditions. Succinylation of the allergens inhibited complex formation, indicating that lysine residues were involved. A 6-fold reduction in IgE binding or allergenic potency of the extract was observed after treatment with phytic acid. It was concluded that phytic acid formed insoluble complexes with the major peanut allergens, and resulted in a peanut extract with reduced allergenic potency. Application of phytic acid to a peanut butter slurry presented a similar result, indicating that phytic acid may find use in the development of hypoallergenic peanut-based products.  相似文献   

6.
The major peanut allergen Ara h 1 is an easily digestible protein under physiological conditions. The present study revealed that pepsin digestion products of Ara h 1 retained the sensitizing potential in a Brown Norway rat model, while this sensitizing capacity was lost by separating the digest into fractions by gel permeation chromatography. Protein chemical analysis showed that the peptide composition as well as the aggregation profiles of the fractions of Ara h 1 digest differed from that of the whole pool. These results indicate that the sensitizing capacity of digested Ara h 1 is a consequence of the peptides being in an aggregated state resembling the intact molecule or that most peptides of the digests need to be present in the same solution, having a synergistic or adjuvant effect and thereby augmenting the immune response against other peptides.  相似文献   

7.
Although many sequences and linear IgE epitopes of allergenic proteins have been identified and archived in databases, structural and physicochemical discriminators that define their specific properties are lacking. Current bioinformatics tools for predicting the potential allergenicity of a novel protein use methods that were not designed to compare peptides. Novel tools to determine the quantitative sequence and three-dimensional (3D) relationships between IgE epitopes of major allergens from peanut and other foods have been implemented in the Structural Database of Allergenic Proteins (SDAP; http://fermi.utmb.edu/SDAP/). These peptide comparison tools are based on five-dimensional physicochemical property (PCP) vectors. Sequences from SDAP proteins similar in their physicochemical properties to known epitopes of Ara h 1 and Ara h 2 were identified by calculating property distance (PD) values. A 3D model of Ara h 1 was generated to visualize the 3D structure and surface exposure of the epitope regions and peptides with a low PD value to them. Many sequences similar to the known epitopes were identified in related nut allergens, and others were within the sequences of Ara h 1 and Ara h 2. Some of the sequences with low PD values correspond to other known epitopes. Regions with low PD values to one another in Ara h 1 had similar predicted structure, on opposite sides of the internal dimer axis. The PD scale detected epitope pairs that are similar in structure and/or reactivity with patient IgE. The high immunogenicity and IgE reactivity of peanut allergen proteins might be due to the proteins' arrays of similar antigenic regions on opposite sides of a single protein structure.  相似文献   

8.
Influence of thermal processing on the allergenicity of peanut proteins   总被引：3，自引：0，他引：3  
Peanuts are one of the most common and severe food allergens. Nevertheless, the occurrence of peanut allergy varies between countries and depends on both the exposure and the way peanuts are consumed. Processing is known to influence the allergenicity of peanut proteins. The aim of this study was to assess the effect of thermal processing on the IgE-binding capacity of whole peanut protein extracts and of the major peanut allergens Ara h 1 and Ara h 2. Whole proteins, Ara h 1, and Ara h 2 were extracted and purified from raw, roasted and boiled peanuts using selective precipitation and multiple chromatographic steps, and were then characterized by electrophoresis and mass spectrometry. The immunoreactivity of whole peanut extracts and purified proteins was analyzed by the enzyme allergosorbent test (EAST) and EAST inhibition using the sera of 37 peanut-allergic patients. The composition of the whole protein extracts was modified after heat processing, especially after boiling. The electrophoretic pattern showed protein bands of low molecular weight that were less marked in boiled than in raw and roasted peanuts. The same low-molecular-weight proteins were found in the cooking water of peanuts. Whole peanut protein extracts obtained after the different processes were all recognized by the IgE of the 37 patients. The IgE-binding capacity of the whole peanut protein extracts prepared from boiled peanuts was 2-fold lower than that of the extracts prepared from raw and roasted peanuts. No significant difference was observed between protein extracts from raw and roasted peanuts. It is noteworthy that the proteins present in the cooking water were also recognized by the IgE of peanut-allergic patients. IgE immunoreactivity of purified Ara h 1 and Ara h 2 prepared from roasted peanuts was higher than that of their counterparts prepared from raw and boiled peanuts. The IgE-binding capacity of purified Ara h 1 and Ara h 2 was altered by heat treatment and in particular was increased by roasting. However, no significant difference in IgE immunoreactivity was observed between whole protein extracts from raw and roasted peanuts. The decrease in allergenicity of boiled peanuts results mainly from a transfer of low-molecular-weight allergens into the water during cooking.  相似文献   

9.
Enzymatic digestion of total protein along with liquid chromatography/tandem mass spectrometry (LC/MS/MS) was used to confirm the presence of a major peanut allergen in food. Several peptides obtained from the enzymatic digestion of the most abundant peanut allergen, Ara h 1, were identified as specific peptide biomarkers for peanut protein. Using ice cream as a model food matrix, a method was developed for the detection of the allergen peptide biomarkers. A key component of the method was the use of molecular mass cutoff filters to enrich the Ara h 1 in the protein extracts. By applying the method to ice cream samples containing various levels of peanut protein, levels as low as 10 mg/kg of Ara h 1 could routinely be detected. This method provides an unambiguous means of confirming the presence of the peanut allergen, Ara h 1, in foods and can easily be modified to detect other food allergens.  相似文献   

10.
The alkali extractable (AE) arabinoxylans from two rye flours differing in baking quality were studied following sequential extraction of water-unextractable and starch-free rye flour residue with saturated barium hydroxide solution, water and 1 M sodium hydroxide solution (Ba, BaH, and Na, respectively), and further fractionation of isolated fractions by ammonium sulfate precipitation. (1)H NMR and sugar analyses of AE subfractions provided evidence for the presence of lowly branched arabinoxylans (average arabinose-to-xylose ratio, Ara/Xyl approximately 0.5), containing mainly un- and monosubstituted xylopyranosyl residues (Xylp) in the chain. The proportion of this subfraction decreased from 50% in the Ba fraction to 35 and 17% in the Na and BaH fractions, respectively. Other subfractions, rich in both mono- and disubstituted Xylp, represented arabinoxylan populations with intermediate (Ara/Xyl approximately 0.8) and high substitution degree (Ara/Xyl approximately 1.1). The Ba and Na fractions contained phenolic compounds, whereas they were absent in the BaH fraction. The higher ratio of such phenolic compounds to arabinose (PhC/Ara) found in AE arabinoxylans from rye flour of inferior baking quality was one of the most pronounced differences between arabinoxylan populations from rye flours with high and low baking quality. The arabinoxylans from rye flour of high baking quality present in Ba and Na fractions had slightly higher apparent molecular weights (MWs) when compared to those from rye flour with low baking quality. The arabinoxylans present in the BaH fractions, characterized by the highest MWs, had similar MWs.  相似文献   

11.
An MS-based method, combining reversed-phase capillary liquid chromatography (capillary LC) with quadrupole time-of-flight tandem mass spectrometry (nano-ESI Q-TOF MS/MS), was developed with the aim of identifying a set of peptides that can function as markers for peanut allergens. Emphasis was given to the identification of the three major peanut allergens Ara h 1, Ara h 2, and Ara h 3, because these proteins are considered to represent >30% of the total protein content of peanut and are directly relevant for the allergenic potential of this food. The analytical data obtained were used to perform databank searching in combination with de novo sequencing and led to the identification of a multitude of sequence tags for all three peanut allergens. Food processing such as roasting of peanuts is known to affect the stability of proteins and was shown to influence the detection of allergen sequence tags. The analysis of raw and roasted peanuts allowed the identification of five peanut-specific sequence tags that can function as markers of the specific allergenic proteins. For Ara h 1, two peptide markers were proposed, namely, VLEENAGGEQEER (m/z 786.88, charge 2+) and DLAFPGSGEQVEK (m/z 688.85, charge 2+), whereas for Ara h 2 only one peptide, RQQWELQGDR (m/z 439.23, charge 3+), was found to satisfy the required conditions. For Ara h 3, the two specific peptides, SPDIYNPQAGSLK (m/z 695.35, charge 2+) and SQSENFEYVAFK (m/z 724.84, charge 2+), were selected. Other peptides have been proposed as indicative for food processing.  相似文献   

12.
Detection of peptides from the peanut allergen Ara h 1 by liquid chromatography-mass spectrometry (LC-MS) was used to identify and estimate total peanut protein levels in dark chocolate. A comparison of enzymatic digestion subsequent to and following extraction of Ara h 1 from the food matrix revealed better limits of detection (LOD) for the pre-extraction digestion (20 ppm) than for the postextraction digestion (50 ppm). Evaluation of LC-MS instruments and scan modes showed the LOD could be further reduced to 10 ppm via a triple-quadrupole and multiple-reaction monitoring. Improvements in extraction techniques combined with an increase in the amount of chocolate extracted (1 g) improved the LOD to 2 ppm of peanut protein. This method provides an unambiguous means of confirming the presence of the peanut protein in foods using peptide markers from a major allergen, Ara h 1, and can easily be modified to detect other food allergens.  相似文献   

13.
Recent studies have indicated that some structural features of arabinoxylans, the major cell wall polysaccharides, might be potential quality markers in the selection of rye breeding materials. To specify the most appropriate characteristics, the differences in the structure of cell wall components were studied in two ryes with high and low breadmaking qualities. Two cell wall fractions were isolated from the outer layers of the grain (pooled shorts and bran fractions) by a consecutive water extraction with alpha-amylase (WE-A) and proteinase K (WE-P). Polysaccharides predominated in the WE-A fraction (approximately 64%, mainly arabinoxylans). By contrast, the WE-P fraction contained mostly protein (approximately 63%), and its level of polysaccharides was relatively low (approximately 18%). The 1H NMR and sugar analysis of the ammonium sulfate precipitated subfractions revealed that the WE-A was built of four arabinoxylan populations with marked structural differences (arabinose-to-xylose ratios, Ara/Xyl, of approximately 0.3, 0.5, 0.8, and 1.2). Instead, the arabinoxylans present in the WE-P were generally enriched in disubstituted xylopyranosyl residues. The ratio of phenolic components to arabinose residues in the WE-P fraction (indicated by 1H NMR) and the proportion of polymers with the highest molecular weights in the WE-A fraction (revealed by HPSEC) distinguished well two ryes with diverse breadmaking qualities. Much less obvious differences between both ryes were observed in the ratio of amide I to amide II band intensities of FTIR spectra for the WE-P and in the level of phenolic acids and ferulic acid dehydrodimers for both cell wall preparations.  相似文献   

14.
Trypsin inhibitors are pathogenesis-related (PR) proteins, which play an important role in the plant defense mechanism against insects and pathogens. Peanut trypsin inhibitors are low molecular mass seed storage proteins. Like peanut allergens, they are stable to acid and heat, resistant to digestion, and can have a negative impact on human health. In peanut, five Bowman-Birk trypsin inhibitors (BBTI) have been isolated and amino acid sequences published. However, to date, no peanut BBTI sequence is available at both the cDNA and the genomic levels. The objectives of this investigation were (i) to synthesize degenerate oligonucleotides based on conserved regions of published amino acid sequences of BBTI, BII, and BIII; (ii) to isolate, sequence, and analyze at least one positive peanut trypsin inhibitor cDNA clone using the synthesized (32)P-labeled oligonucleotides as probes; and (iii) to determine its trypsin inhibitory activity. Thirty-two degenerate oligonucleotides DNA primers of 24 nucleotides each were synthesized based on the published amino acid sequences of peanut BBTI, and two were selected as probes to screen a peanut Lambda gt 11 cDNA library. Three putative positive clones were isolated, purified, and subcloned, and one was sequenced. Sequence analysis revealed a partial cDNA clone of 643 bp with a start codon. This clone shares 93 and 96% nucleotide sequence homology with peanut allergens Ara h 3 and Ara h 4 cDNA clones, respectively. A trypsin inhibitor assay revealed that peanut allergen Ara h 3 has a trypsin inhibitory activity of 11 238 TIA/mg protein. We concluded that peanut allergen Ara h 3 may also function as a trypsin inhibitor.  相似文献   

15.
Looking for potential quality indicators, which could be used in early selection of breeding materials, the structural features of cell wall arabinoxylans (AX) from outer layers of the grain (pooled shorts and bran fractions) were studied in two ryes with diverse breadmaking quality. The successive alkaline extraction of water-unextractable material with saturated Ba(OH)2, followed by water and 1 and 4 M NaOH, resulted in four purified fractions, Ba, BaH, 1Na, and 4Na, respectively, that became water soluble after their isolation. The AX present in these fractions constituted approximately 43, 12, 14, and 4% of their total amount recovered. Moreover, two xylan-enriched fractions, 1Na.P and 4Na.P (arabinose-to-xylose ratios, Ara/Xyl, of 0.07 and 0.19, respectively), were self-precipitated from both NaOH-extractable fractions. Polysaccharides of these fractions, containing mainly xylose, represented approximately 16 and 1% of AX recovered. In the BaH and 1Na, AX coexisted with beta-glucans, which predominated in the former protein-free fraction. On the contrary, hemicelluloses in the 1Na fraction were associated with protein as well. Further fractionation of the water-soluble materials by ammonium sulfate revealed that the parent AX populations in the Ba, BaH, and 1Na were composed of 3-4 subfractions with different degrees of substitution (Ara/Xyl of approximately 0.4, 0.8, and 1.1), whereas 4Na was almost totally built of highly substituted AX (Ara/Xyl of 1.1). Despite a comparable proportion of un-, mono-, and disubstituted xylopyranosyl residues in the chain of Ba(OH)2-extractable AX isolated from both ryes, the 1H NMR and Fourier transform infrared demonstrated the marked differences in their spectral profiles, suggesting different substitution patterns of these dominating polysaccharides. The high molecular weight population present in the Ba fraction also differentiated well two ryes with opposite breadmaking quality.  相似文献   

16.
Water-soluble arabinoxylans from wheat flour were purified and fractionated by graded ethanol precipitation. Six fractions were obtained at 20% (F20), 30% (F30), 40% (F40), 50% (F50), 60% (F60), and 70% (F70) saturation with ethanol. Neutral sugars and (1)H NMR analyses revealed differences in structural characteristics. The Ara/Xyl ratio and the amount of Xylp residues disubstituted increased with ethanol concentration. Ferulic acid content was higher in fractions precipitated at low ethanol percentage. Fractions were refractionated by SEC, leading to 46 subfractions with low polydispersity index. Substitution degree was apparently linearly related to the amount of disubstituted Xylp. Macromolecular characteristics (M(w), [eta], R(G), q, nu) determined by multiangle laser light scattering and viscosimetry were similar among all fractions. A rather flexible conformation was determined for the arabinoxylans, in conflict with the admitted rodlike conformation. The substitution degree had no influence on the conformation or on the rigidity of the polymers. Evidence for the presence of ferulic acid dimers in the water-soluble arabinoxylans is provided, which probably explains the unexpected conformation and macromolecular characteristics.  相似文献   

17.
电子束辐照对花生过敏原免疫原性及生化性质影响的研究   总被引：2，自引：0，他引：2  
研究了电子束辐照降低花生过敏原免疫原性的效果及辐照对花生生化性质的影响。选择2、4、6、8、10、15和20kGy剂量的电子束对花生过敏原液、脱脂花生粉进行辐照处理,辐照后花生主要过敏原(Ara h 1, Ara h 2, Ara h 3)蛋白分子质量的变化通过SDS-聚丙烯酰胺凝胶电泳测定,免疫原性的变化通过免疫印迹和间接竞争ELISA法测定;辐照后花生过敏原溶液的浓度、浊度及疏水性的变化通过紫外分光光度计和荧光光度计分别进行测定。结果表明,花生过敏原在溶液状态比固体状态对辐照更为敏感。当辐照剂量低于10kGy时处理的过敏原液的免疫原性稍有增强,剂量大于10kGy时免疫原性降低,剂量为20kGy时过敏原液的IC50值是未处理的11倍。辐照使过敏液的浓度和浊度随着剂量的加大而增加,疏水性与对照组相比增强,但当剂量大于15kGy时降低。电子束辐照改变了过敏原的生化性质,降低了其免疫原性,比较而言,辐照对液体状态下过敏原的影响更显著。  相似文献   

18.
Ara h 1, a major peanut allergen, is known as a stable trimeric protein. Nevertheless, upon purification of native Ara h 1 from peanuts using only size exclusion chromatography, the allergen appeared to exist in an oligomeric structure, rather than as a trimeric structure. The oligomeric structure was independent of the salt concentration applied. Subjecting the allergen to anion exchange chromatography induced the allergen to dissociate into trimers. Ammonium sulfate precipitation did not bring about any structural changes, whereas exposing the allergen to hydrophobic interaction chromatography caused it to partly dissociate into trimers, with increasing amounts of trimers at higher ionic strengths. The (partial) dissociation into trimers led to a change in the tertiary structure of the monomeric subunits of the allergen, with the monomers in Ara h 1 oligomers having a more compact tertiary structure compared with the monomers in Ara h 1 trimers. As structural characteristics are important for a protein's allergenicity, this finding may imply a different allergenicity for Ara h 1 than previously described.  相似文献   

19.
The influence of thermal processing and nonenzymatic browning reactions on the IgE-binding activity of rAra h 2 was studied and compared to findings recently reported for the allergen's natural counterpart. ELISA experiments as well as inhibition assays revealed that thermal treatment of rAra h 2 in the presence of reactive carbohydrates and carbohydrate breakdown products induces a strong increase of the IgE-binding activity, thus collaborating with the data reported for the natural protein isolated from peanuts. To localize the Ara h 2 sequences responsible for the formation of highly IgE-affine glycation sites, model peptides have been synthesized mimicking sequences which contain possible targets for glycation as well as the immunodominant epitopes. Immunological evaluation of these peptides heated in the absence or presence of reducing sugars and carbonyls, respectively, revealed that neither the two lysine residues of Ara h 2 nor its N-terminus are involved in the formation of IgE-affine structures by Maillard reaction. Also, the cysteine-containing major epitope 3 (aa 27-36) was found to lose its IgE-binding capacity upon heating. By contrast, the overlapping major epitopes 6 and 7, which do not contain any lysine or arginine moieties, showed a distinct higher level of IgE binding when subjected to Maillard reaction, thus giving the first evidence that nonbasic amino acids might be accessible for nonenzymatic glycation reactions and that these posttranslational modifications might induce increased IgE binding of the glycated Ara h 2. Analogous experiments were performed with peanut agglutinin, considered in the literature as a minor allergen. ELISA experiments revealed that the majority of tested sera samples from peanut-sensitive patients showed a high level of IgE binding to the lectin even after heat treatment. In contradiction to published data, nonenzymatic browning reactions seem to deteriorate the IgE affinity of the lectin.  相似文献   

20.
Hidden allergens in food products are, especially for peanut-allergic consumers, a serious problem because even low amounts (approximately 200 microg) of peanut can elicit allergic reactions. Undeclared peanut traces can be found in processed food products, because contaminations with peanut during production processes are frequent. To minimize the risk of such cross-contaminations, it is necessary to develop sensitive analytical methods for the detection of hidden allergens in foods. For this approach we developed two peanut-specific assays based on the detection of peanut protein by specific antibodies (sandwich ELISA) and by the detection of peanut-specific DNA (part of the coding region of Ara h 2) by a real-time PCR. Both tests did not show any cross-reactivity with 22 common food ingredients (cereals, nuts, legumes), and the limit of detection is <10 ppm peanut in processed foods. Thirty-three random samples of food products were tested for the presence of peanut to compare both assay types with each other and to evaluate the percentage of foods on the German market that are contaminated with peanut traces. We found that four products (13.3%) without peanut in the list of ingredients contained peanut protein in a range from 1 to 74 ppm peanut protein and that the results of both tests correlated well. The real-time PCR was able to detect one more positive sample than the sandwich ELISA. In conclusion, both assays are sensitive and specific tools for the detection of hidden allergens in processed foods.  相似文献   

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