大豆过敏原夹心ELISA和竞争ELISA方法的建立及其在加工食品中应用研究

本文以大豆混合过敏原为目标,建立了快速、便捷检测大豆过敏原的夹心酶联免疫吸附方法（sandwich-enzyme linked immunosorbent assay）和间接竞争酶联免疫吸附方法（indirect competitive enzyme-linked immunosorbent assay）,通过实际加工样品的回收实验、加标食品回收实验以及对真实食物样本的检测,对这两种方法进行了比较,确定了各自的适用范围。结果表明,夹心ELISA方法标准品浓度在0.0078~30 μg/mL范围内呈现出良好的线性关系,曲线方程为y=0.2333x+0.0692,决定系数R2=0.995。竞争ELISA方法的检测范围为10~100000 ng/mL,最低检测限为10 ng/mL。对购入橙汁进行加标回收实验,夹心ELISA检测后的回收率要高于竞争ELISA检测后的回收率,达100%以上;而对成分和加工方式都比较复杂的巧克力、牛肉酱、面包或蛋糕来说,竞争ELISA检测后的回收率要高于夹心ELISA检测后的回收率。对发酵类食物进行检测,竞争ELISA方法检测到的浓度要高于夹心ELISA,而对成分比较简单的食物比如芝麻糊、豆奶等进行检测时,夹心ELISA的检测浓度要略高于竞争ELISA。综上,竞争ELISA方法更适用于食物基质复杂,经过深度加工的食品,而夹心ELISA方法更适用于食物成分简单,轻加工后的食品,两种方法在各自的适用范围内均能实现较准确的检测。     

Validation and comparison of a sandwich ELISA,two competitive ELISAs and a real-time PCR method for the detection of lupine in food

Methods applied in food allergen analysis should be specific, sensitive and applicable to both raw and highly processed foods. The performance of the most commonly used methods, ELISA and real-time PCR, may, however, be influenced by food processing steps, e.g., heat treatment. The present study compares the applicability of four in-house developed methods, one sandwich ELISA, two competitive ELISAs and a real-time PCR method, for the detection of lupine in four different food matrices, comprising bread, biscuits, rice patties and noodles. In order to investigate the influence of food processing on the detectability, not only the heat treated model foods but also the corresponding doughs were analysed. The sandwich ELISA proved to be the most sensitive method. The LOD was found to be 10 ppm lupine, independent from the food matrix and independent if the dough or the heat treated food was analysed. In addition, the methods were applied to the analysis of commercial foodstuffs differing in their labelling.     

Commercial soybean lecithins: a source of hidden allergens?

 Soybeans are known to be allergenic for adults as well as for infants. Processed products derived from soybeans are used in a wide spectrum of foods, drugs and other industrial products. In particular, soybean lecithins are used as stabilizers and emulsifiers and may not be suspected as possible source of allergens. To test this hypothesis, six commercial soy lecithins were investigated for residual allergenicity and compared with extracts from raw and heat-treated soybeans. They were characterized, the protein content was determined by enzyme-linked immunosorbent assay (ELISA) and allergens were analyzed with specific IgE from patients' sera using the enzyme allergosorbent test (EAST), EAST inhibition and protein blotting followed by immunodetection. For further characterization a polyclonal antiserum directed against soybean extract and a monoclonal antibody (mAb 025) directed against the acidic subunit of the soybean storage protein glycinin were used. The EAST studies revealed that three of six sera from patients with allergy to soybeans contained IgE to four soy lecithins (Topcithin 50, Topcithin 300, Emulfluid FD 12, Epikuron 100 P), the same lecithins which were found to contain residual proteins. Two lecithins with a protein content of less than 20 ppb did not bind IgE. EAST inhibition showed that the allergens from soy lecithin were immunologically more closely related to allergens from heat-treated soybeans than to those from raw soybeans. Protein blotting and immunodetection of the protein extract from the lecithins resulted in various allergen bands between 14 kDa and 94 kDa. A heat-stable allergen of 39 kDa was recognized by the monoclonal antibody and thus identified as a subunit of glycinin. The results obtained were confirmed by a mediator release assay based on a rat basophil leukemia cell line. Lecithins that contained residual proteins caused a specific mediator release, suggesting that these products may induce allergic symptoms. Our results show that soybean lecithins are capable of introducing hidden allergens to processed foods and that the IgE binding potential corresponds to the total protein determined by ELISA. Furthermore, it appears to be possible that by monitoring the protein content soy lecithins can be applied which may be safe for the allergic consumer. Received: 22 January 1998     

Validated sandwich enzyme-linked immunosorbent assay for casein and its application to retail and milk-allergic complaint foods

Cows' milk is a commonly allergenic food. Cross-contamination of milk proteins into nondairy, kosher-pareve foods prepared on shared processing equipment can cause severe, life-threatening reactions in milk-allergic individuals. A sandwich-type enzyme-linked immunosorbent assay (ELISA; 96-well plate format) was developed for the detection of undeclared casein in foods. Rabbit anti-casein antibodies were used as the capture reagent. Food samples and standards were ground, extracted in 0.01 M phosphate-buffered saline, clarified by centrifugation, and added to the wells. Goat anti-casein antibodies were employed as the detector antibody, and the amount of antibody bound was determined with a commercial rabbit anti-goat immunoglobulin conjugated to alkaline phosphatase, with subsequent substrate reaction. Antibodies developed were specific to casein, with no cross-reaction observed with 30 foods and food ingredients. Non-milk-containing products such as fruit juices, fruit juice bars, sorbets, and dark and pareve-labeled chocolate were purchased from June 2002 through June 2003. In addition, samples allegedly causing eight milk-allergic consumer complaints were analyzed. The ELISA had a detection limit of less than 0.5 ppm of casein. The casein content in the analyzed foods ranged from less than 0.5 ppm to more than 40,000 ppm casein; undeclared casein residues were found in all of the samples implicated in allergic reactions. The levels of milk contamination in some of the other surveyed products could also be hazardous for milk-allergic consumers. This ELISA method provides a useful quality control tool for the food industry and could also be used as a validation of kosher-pareve status.     

Survey of undeclared soy allergen levels in the most frequently recalled food categories with or without precautionary labelling

A comprehensive study was designed to determine the frequency and levels of soy allergen in packaged bakery and snack food products. A representative sample of products with no soy allergen disclosed on the label was analysed using two widely used enzyme-linked immunosorbent assay (ELISA) methods. Samples were chosen that either had no soy identified on the product label or which had a soy precautionary statement. Among 558 bakery and snack products, soy protein was detected in 17% of the products using the Neogen (NE) kit and 11% of the products using the Elisa Systems (ES) kit. The disagreement rates between kits were 8.8% for bakery products and 3.3% for snack products. Overall soy protein was detected at higher frequency in bakery products than in snack foods. Among 284 bakery samples, soy protein was detected in 25% of the samples with no precautionary statement and 19% of the samples which had a precautionary statement. Among 274 snack samples, soy protein was detected in 11% of the samples with no precautionary statement and 9% of the samples which had a precautionary statement. The sample repeatability was at an acceptable level (< 9%) for each method and food commodity. The reproducibility between kits was 23% for bakery foods and 36% for snack foods. None of the bakery (21) and snack (6) products without precautionary labelling (measured level > 5 ppm) had a higher level of soy protein per serving compared with the eliciting dose₁₀ (ED₁₀) of 10.6 mg for soy allergic patients. But the level of soy protein per serving may be clinically relevant to a subpopulation of soy allergic patients if a more stringent eliciting dose is applied. These findings emphasise that suitable detection methodologies and references doses are crucial for labelling accuracy and the safety of soy allergic consumers.     

Sandwich Enzyme‐Linked Immunosorbent Assay (ELISA) for the Detection of Lupine Residues in Foods

ABSTRACT: Lupine has been increasingly used in food applications due to its high nutritional value and excellent functional properties. However, lupine provokes allergic reactions in susceptible individuals. The presence of undeclared lupine residues in foods can pose a serious health risk to lupine‐allergic individuals. Therefore, the objective of this research was to develop a sandwich‐type ELISA for the detection of lupine residues in foods. Lupine flour derived from Lupinus albus was used to immunize 3 rabbits and a sheep. Pooled lupine‐specific antibodies were partially purified from the sera by ammonium sulfate precipitation. A sandwich lupine ELISA with a limit of quantification (LOQ) of 1 ppm was developed by utilizing the rabbit antisera as the capture reagent and the sheep antiserum as the detector reagent. The binding of the antigen‐antibody complex was visualized by the addition of commercial rabbit antisheep IgG antibody labeled with alkaline phosphatase with subsequent addition of p‐nitrophenyl phosphate substrate to produce a colored product for quantification. Minor cross‐reactivity was observed with soy (Glycine max) and black bean (Castanospermum australe). The performance of the lupine ELISA was evaluated in reference food standards (beef frankfurter and apple cinnamon muffin) and laboratory‐prepared cooked frankfurters and corn muffins. The mean percent recovery for lupine spiked‐frankfurters and corn muffins were 108.4%± 8.8% and 103.1%± 11.5%, respectively. The sandwich‐type lupine ELISA developed in this study provides food manufacturers and regulatory agencies with an effective analytical tool to detect and quantify lupine residues in processed foods.     

Development and validation of a sandwich ELISA for the determination of potentially allergenic lupine in food

The paper presents a sandwich enzyme linked immunosorbent assay (ELISA) for the detection of traces of lupine proteins in foods. Anti-lupine antibodies were produced by immunising a rabbit and a hen with a protein extract from white lupine flour. IgY were used as coating and IgG as secondary antibodies. The ELISA detects proteins from white (Lupinus albus) and blue (Lupinus angustifolius) lupine and, with a lower sensitivity, proteins from yellow (Lupinus luteus) lupine. The ELISA does not show any cross-reactivity with 34 plant species potentially used in lupine containing foodstuffs. Accuracy, repeatability, limit of detection (LOD) and limit of quantification (LOQ) were determined by analysing model biscuits and noodles containing from 0 to 10,000 ppm lupine flour. Lupine flour could be detected in the unprocessed doughs as well as in the processed products down to a spiking level of 1 ppm.     

Detection and isolation of Escherichia coli with a coding gene for enteroaggregative Escherichia coli heat-stable enterotoxin 1 from food and comparison with fecal isolates

Enteroaggregative Escherichia coli heat-stable enterotoxin 1 (EAST1) was originally regarded as a putative enterotoxin of enteroaggregative Escherichia coli. Although its etiological role has not yet been elucidated, it has been epidemiologically suggested that some strains of E. coli possessing EAST1-coding gene (astA) but no other identifiable pathogenic properties comprise a new group of diarrhea-associated E. coli (EAST1EC). However, the source of the organisms and their prevalence in foods are still obscure. In this study, methods for detection of the organisms in foods heavily contaminated with coliforms were evaluated and properties of the isolated strains were compared with those of fecal strains. Four enrichment methods (brilliant green lactose bile broth, E. coli, lauryl tryptose broth, and a combination of brain heart infusion broth and tryptone phosphate broth) were evaluated through inspection of 115 samples. PCR showed positive results in 26 samples after enrichment with a combination of brain heart infusion broth and tryptone phosphate broth, and EAST1EC was successfully isolated from 18 samples. Fifteen samples showed a positive reaction in the PCR test after enrichment by the other methods, and the organisms were isolated from only 10 specimens. The highest prevalence of EAST1EC was found in animal products (16 of 54, 29.6%); the organism was rarely found in foods of plant origin (2 of 45, 4.4%) or fishery products (1 of 16, 6.3%). Although EAST1EC is unexpectedly common in animal products, its potential as a human pathogen remains uncertain because the possession of some virulence properties differs significantly between strains from fecal specimens and those from foods. Some food isolates, however, possess the same characteristics as diarrheal isolates do. It is necessary to clarify the pathogenicity of EAST1EC and the significance of food as a source of infection.     

花生过敏原检测方法研究进展

花生是重要食物过敏原之一,能引起严重的过敏反应。目前尚没有花生过敏的特效疗法,严格避免食入含花生的食物是花生过敏患者的最佳选择,所以食物中花生的检测就显得尤为重要。本文对花生主要过敏原及其过敏反应研究进展进行简要介绍,重点介绍花生过敏原的主要检测方法的新发展,包括传统的酶联免疫吸附实验(ELISA)、免疫印迹法、聚合酶链式反应(PCR)等,ELISA和免疫印迹法都是应用较为普遍的检验方法,PCR方法应用较少,但它能从DNA/RNA方面检测花生过敏原的存在;新兴检测方法主要包括生物传感器和质谱法,这两种方法在花生检测方面具有可观的前景。未来的这些检测方法将朝着快速、灵敏、简便的方向发展。     

Validation of end-point and real-time PCR methods for the rapid detection of soy allergen in processed products

This work describes the development and validation of two PCR methods, end-point and real-time PCR, for the detection of soy protein in a wide rage of foodstuffs. These techniques are reliable and sensitive, allowing detection of trace amounts of soybean in processed products. TaqMan real-time PCR was the simpler and more rapid process, with a higher potential for automation and, therefore, currently the most suitable screening method. To verify correct operation of the proposed methodology, ELISA was used for quantitative determination of soy protein. In addition, 35 meat, fish and bakery processed products, which could potentially contain soy but was not declared on the label, were tested for the presence of soy DNA using the proposed methods. The methodologies will be valuable in issues regarding the presence of soy protein in processed products, especially in verifying labelling and security regulations to protect consumer's rights.     

Development of real-time PCR assays for the detection of lupin residues in food products

Lupin is a legume from the Leguminosae family that is used, amongst other, for human nutrition. In Europe, lupin is used as a substitute for soy in bakery and dietary products and recently its consumption has increased significantly. Unfortunately lupin is known to trigger allergic reactions in sensitised individuals and therefore its use in food products requires a mandatory declaration on the label in accordance with Directive 2007/68/EC. To protect the allergic consumer the availability of detection methods for the identification of lupin in food products is required. Here we present the development of two real-time polymerase chain reaction (PCR) methods that allow the detection of lupin-specific DNA as a marker for the presence of this allergenic ingredient in food products. Genomic DNA sequences coding for conglutin genes were chosen as targets for the detection of lupin. One primer set and probe was designed for the amplification of a 153 bp fragment of α-conglutin; another primer set and probe was designed for the detection of a 150 bp δ-conglutin amplicon. Lupin at a level of 10 mg/kg food matrix could be detected in cookies baked from a lupin containing dough using the α-conglutin method. Since lupin is used in bakery products the effects exerted by heat treatments on lupin detection by real-time PCR have been investigated. Enzyme-linked immunosorbent assay (ELISA) analyses were performed in parallel to compare the detection of lupin DNA with that of lupin protein in market products. Qualitative ELISA results confirm results obtained by the real-time PCR methods targeting α- and δ-conglutin.     

Quantification of Human IgE Immunoreactive Soybean Proteins in Commercial Soy Ingredients and Products

ABSTRACT:  The objective of this study was the detection and quantification of human IgE immunoreactive soybean proteins in commercially available soy ingredients and products. Optimum dilutions of primary antibody and antigens as well as detection sensitivity were determined for the implementation of a sandwich ELISA method using plasma from soy sensitive subjects (IgE ranging from 0.35 to 98.7 IU/mL). Human IgE immunoreactivity of commercial soybean ingredients showed that the plasma of subjects with strong allergic reaction to soybean presented proportionally higher immunoreactive response. Soy protein isolate and soy protein concentrate contained less immunoreactive proteins than soy flour and grits. As expected, a hypoallergenic soybean product presented the lowest IgE immunoreactivity. Hydrolyzed and fermented soy ingredients showed negligible human IgE immunoreactivity when proteins and peptides were < 20 kDa. The IgE immunoreactivity of soymilk samples ranged from 3.4 to 68.9 ng IgE/mg extracted protein. Tofu contained about 20-fold higher IgE immunoreactivity than soymilk products (median 171 ng IgE/mg extracted protein). Furthermore, soy cheese products presented twice the IgE immunoreactivity than tofu products (median 359 ng IgE/mg protein). Meat analogues presented considerably high extracted protein concentration (median 67.9 mg/g product). The findings of the current investigation demonstrate sandwich ELISA as a reliable immunochemical method with good repeatability, sensitivity, and low detection limit to quantify IgE immunoreactive proteins in soy ingredients and products. Quantitative measurement of specific IgE is likely to become an increasingly valuable tool for soybean industry to comply with food labeling for manufacturers, thus protecting soy-sensitive consumers.     

直接竞争酶联免疫吸附法检测虾过敏蛋白

目的:建立酶标抗原的直接竞争酶联免疫吸附法(dcELISA)检测食品中虾过敏蛋白,为食品过敏诊断试剂的开发和应用提供理论基础。方法:提取虾主要过敏蛋白,免疫小鼠制备抗虾过敏蛋白多克隆抗体,辣根过氧化物酶(HRP)标记抗原,建立酶标抗原的dcELISA检测虾过敏蛋白。结果:所建立的dcELISA法最低检测限为3.94ng/mL,标准曲线在0.12～128.86ng/mL范围内线性良好,批内和批间变异系数分别为6.16%和2.73%,回收率为82%～98%。结论:该方法具有良好的特异性、敏感性和稳定性,为进一步研制检测虾过敏蛋白的ELISA试剂盒提供有效的方法。     

Application of a qualitative and quantitative real-time polymerase chain reaction method for detecting genetically modified papaya line 55-1 in papaya products

Genetically modified (GM) papaya (Carica papaya L.) line 55-1 (55-1), which is resistant to papaya ringspot virus infection, has been marketed internationally. Many countries have mandatory labeling regulations for GM foods, and there is a need for specific methods for detecting 55-1. Here, an event- and construct-specific real-time polymerase chain reaction (PCR) method was developed for detecting 55-1 in papaya products. Quantitative detection was possible for fresh papaya fruit up to dilutions of 0.001% and 0.01% (weight per weight [w/w]) for homozygous SunUp and heterozygous Rainbow cultivars, respectively, in non-GM papaya. The limit of detection and quantification was as low as 250 copies of the haploid genome according to a standard reference plasmid. The method was applicable to qualitative detection of 55-1 in eight types of processed products (canned papaya, pickled papaya, dried fruit, papaya-leaf tea, jam, puree, juice, and frozen dessert) containing papaya as a main ingredient.     

Detection of Walnut Residues in Foods Using an Enzyme-Linked Immunosorbent Assay

ABSTRACT:  Tree nuts, including walnuts, can be responsible for allergic reactions. Food manufacturers have the responsibility to declare the presence of walnuts on packaged foods even when trace residues may be present from the use of shared equipment or the adventitious contamination of ingredients. The aim of this study was to develop a rapid, sensitive, and specific enzyme-linked immunosorbent assay (ELISA) method for the detection of walnut protein residues. Mixtures of raw and roasted English walnuts of several varieties were defatted, powdered, and used as separate antigens in sheep and New Zealand white rabbits. An ELISA was developed using the sheep antiroasted walnut serum as the capture reagent and rabbit antiroasted walnut serum as the detector reagent followed by addition of commercial goat anti-rabbit IgG antibody labeled with alkaline phosphatase and subsequent substrate addition. The performance of the ELISA was validated by testing known amounts of walnut (0 to 100 ppm) either spiked into or manufactured into milk chocolate, cookies, muffins, or ice cream. Recoveries of 1 to 100 ppm walnut-in-chocolate ranged from 71.6% to 119%± 7% to 16.5%. The walnut ELISA has a detection limit of 1 ppm (1 μg/g) walnut in several food matrices. Substantial cross-reactivity was observed with pecan while minimal cross-reactivity was noted for hazelnut, mustard, mace, and poppy seed among almost 100 foods and food ingredients tested. This walnut ELISA can be used to detect undeclared walnut residues in foods and ingredients and as a tool to validate the effectiveness of allergen control programs for walnuts.     

Development of two immunoassay formats to detect beta-lactoglobulin: influence of heat treatment on beta-lactoglobulin immunoreactivity and assay applicability in processed food

Milk proteins are commonly used as ingredients in the food industry because of their functional properties, but they can cause severe reactions in milk-allergic individuals. In this work, two enzyme-linked immunosorbent assay (ELISA) formats were developed to detect bovine beta-lactoglobulin. The indirect competitive ELISA involved the use of anti-beta-lactoglobulin antisera, and the sandwich ELISA involved the use of specific antibodies isolated using a beta-lactoglobulin immunosorbent material. The effect of heat treatment on immunoreactivity of the protein in buffer and in milk was determined with both assays. The amount of immunoreactive protein in buffer and in milk decreased as determined by the sandwich ELISA, whereas the amount increased when measuring with the competitive ELISA. Several food products, including meat, bakery products, sauces, and snacks, were analyzed. With both assays, 10 of 11 products in which the ingredient list included the terms "powdered milk" or "milk proteins" contained beta-lactoglobulin. However, the beta-lactoglobulin concentration in these products obtained with the competitive ELISA were much higher than those obtained with the sandwich ELISA. These differences could be explained by the fact that the determination of beta-lactoglobulin concentration by immunoassay is influenced by differences in antibody recognition of the protein present in highly processed foods. Therefore, the antigen-binding properties of antibodies used in a particular immunoassay are important for a correct interpretation of results obtained in food processed at high temperature.     

Immunoassays for Bowman-Birk and Kunitz Soybean Trypsin Inhibitors in Infant Formula

ABSTRACT: Because the consumption of soybean inhibitors of digestive enzymes in processed foods may have both beneficial and adverse health-related effects, reliable and rapid analytical methods for these inhibitors are needed. Monoclonal antibody-based sandwich enzyme-linked immunosorbent assays (ELISAs) were developed for the 2 major soybean protease inhibitors, the Kunitz trypsin inhibitor (KTI) and Bowman-Birk inhibitor (BBI) of trypsin and chymotrypsin. The ELISAs had limits of quantification of approximately 1 and 3 ng/mL for BBI and KTI, respectively, and were used to measure active inhibitors in soy infant formulas. Results were compared with enzymatic analyses and demonstrated that most of the trypsin- and chymotrypsin-inhibitory activities of infant formula were due to constituents other than KTI and BBI. The sandwich ELISA for BBI was also effective in detecting soybean germplasm with atypically low levels of BBI.     

RIDASCREEN® FAST PEANUT, a rapid and safe tool to determine peanut contamination in food

During the last years allergenic substances in food have gained more and more attention. Stricter rules for a peanut free food labelling demand a peanut contamination less than 5 ppm. The maintenance of a high quality of food products with regards to allergenic exposure is preferable warranted with rapid tests that can be utilized as an aid for suppliers to control raw materials, to avoid cross contamination during production and to check the final products. A rapid sandwich peanut ELISA was developed, which covers a measuring range of 2.5–20 ppm peanut (detection limit of 1.5 ppm). This test was successfully evaluated in an independent study under the supervision of the AOAC Research Institute, getting the AOAC certificate No. 030404. In‐house validation and independent validation data demonstrate the reliability, accuracy and precision of the test.     

Effect of proteolysis during Cheddar cheese aging on the detection of milk protein residues by ELISA

Cow milk is a common allergenic food, and cow milk-derived cheese retains an appreciable level of allergenicity. The specific and sensitive detection of milk protein residues in foods is needed to protect milk-allergic consumers from exposure to undeclared milk protein residues contained in foods made with milk or milk-derived ingredients or made on shared equipment or in shared facilities with milk or milk-derived ingredients. However, during cheese ripening, milk proteins are degraded by chymosin and milk-derived and bacterial proteases. Commercial allergen-detection methods are not validated for the detection of residues in fermented or hydrolyzed products. The objective of this research was to evaluate commercially available milk ELISA kits for their capability to detect milk protein residues in aged Cheddar cheese. Cheddar cheese was manufactured at a local dairy plant and was aged at 5°C for 24 mo, with samples removed at various time points throughout aging. Milk protein residues and protein profiles were measured using 4 commercial milk ELISA kits and sodium dodecyl sulfate-PAGE. The ELISA data revealed a 90% loss of milk protein residue signal between the youngest and oldest Cheddar cheese samples (0.5 and 24 mo, respectively). Sodium dodecyl sulfate-PAGE analysis showed protein degradation throughout aging, with the highest level of proteolysis observed at 24 mo. Results suggest that current commercial milk ELISA methods can detect milk protein residues in young Cheddar cheese, but the detection signal dramatically decreases during aging. The 4 evaluated ELISA kits were not capable of detecting trace levels of milk protein residues in aged cheese. Reliable detection of allergen residues in fermented food products is critical for upholding allergen-control programs, maintaining product safety, and protecting allergic consumers. Furthermore, this research suggests a novel use of ELISA kits to monitor protein degradation as an indication of cheese ripening.     

食品过敏原检测技术研究进展

目前食物过敏在人群中的収生率呈明显上升趋势,食物过敏已成为突出的食品安全问题。食物过敏事敀最有敁的预防方式是过敏者避克食用过敏食物,因此检测不同食物中是否含有过敏原其有十分重要的意义。本文比较了食品法具委员会、澳大利亚、加拿大、中国、欧盟、日本、南非、美国对食品过敏原标识管理的情况,综述了基于蛋白水平的酶联克疫(enzyme-linked immuno sorbent assay, ELISA)法、克疫层析技术和基于核酸水平的实时荧光定量PCR技术、环介导等温扩增技术(loop-mediated isothermal amplification, LAMP)检测食物过敏原的方法,探讨了质谱法以及生物芯片、生物传感器等兵他新关检测技术在过敏原检测领域的应用,有利于加强食品质量监管的力度,确保食品安全。