Immunochemical Identification and Quantification of Ovalbumin Additive in Canned Mushrooms

Breton, C.; Thanh, Luu Phan; Paraf, A

doi:10.1111/j.1365-2621.1988.tb10215.x

Cited by 22 publications

(5 citation statements)

References 18 publications

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“…Techniques need to be designed which are applicable to recently introduced technologies such as heat treatment at high temperatures (between 70°C and 130°C). Using ovalbumin as a model we have confirmed the observations of Kilshaw et al (1986) (Breton et al, 1988a) and have shown that polyclonal antibodies can detect ovalbumin which has been used as an additive in canned mushrooms heated to 130°C (Breton et al, 1988b). We were interested in obtaining information on the real structure of the heat-denatured ovalbumin (HDOA) in such complex media; it may be present as pure monomeric (mHDOA) or polymeric (pHDOA) molecules or as a complex with other molecules such as mono or polysaccharides present in the medium.…”

Section: Introductionsupporting

confidence: 87%

Structure of Native and Heat‐denatured Ovalbumin as Revealed by Monoclonal Antibodies: Epitopic Changes during Heat Treatment

Varshney

Mahana

Filloux

et al. 1991

Journal of Food Science

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Twenty-one monoclonal antibodies (MAbs) of IgG, or IgM isotype were developed against either native or heat denatured ovalbumin. Most of the anti-native ovalbumin MAbs were of the IgGr isotype and had high affinity for native ovalbumin in a sandwich ELISA test (antigen bound by immunocapture with polyclonal antibodies). Anti-native MAbs did not recognize plastic bound ovalbumin in an indirect ELISA. Most anti-heat denatured ovalbumin MAbs were of the IgM isotype and reacted with ovalbumin on plastic but not with ovalbumin in the sandwich ELISA test. An immunocapture test using these MAbs was developed which enabled determination of temperatures to which ovalbumin had previously been heated.

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Section: Introductionsupporting

confidence: 87%

Structure of Native and Heat‐denatured Ovalbumin as Revealed by Monoclonal Antibodies: Epitopic Changes during Heat Treatment

Varshney

Mahana

Filloux

et al. 1991

Journal of Food Science

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“…For instance, earlier studies reported the quantification of ovalbumin in canned foods and dairy-based foods , as well as the detection of other egg proteins in a wide range of egg-containing processed foods , using ELISAs. A relevant study reported the successful development of a sandwich ELISA method for the detection of residual ovalbumin in pasta products, a method deemed to be useful for routine monitoring in industrial cleanup operations .…”

Section: Egg Allergy and Industrial Perspectivesmentioning

confidence: 99%

Recent Advances in the Understanding of Egg Allergens: Basic, Industrial, and Clinical Perspectives

Mine

Yang

2008

J. Agric. Food Chem.

167

123

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The emergence of egg allergy has had both industrial and clinical implications. In industrialized countries, egg allergy accounts for one of the most prevalent food hypersensitivities, especially in children. Atopic dermatitis represents the most common clinical manifestation in infancy; however, the range of clinical signs is broad and encompasses life-threatening anaphylaxis. The dominant egg allergens are proteins and are mainly present in the egg white, for example, ovalbumin, ovomucoid, ovotransferrin, and lysozyme. However, egg yolk also displays low-level allergenicity, for example, alpha-livetin. Strict avoidance of the offending food remains the most common recommendation for egg-allergic individuals. Nevertheless, the omnipresence of egg-derived components in prepackaged or prepared foods makes it difficult. Therefore, more efficient preventive approaches are investigated to protect consumers from inadvertent exposure and ensuing adverse reactions. On the one hand, commercial kits have become readily available that allow for the detection of egg contaminants at trace levels. On the other hand, attempts to produce hypoallergenic egg-containing products through food-processing techniques have met with promising results, but the approach is limited due to its potentially undesirable effects on the unique functional and sensory attributes of egg proteins. Therefore, the development of preventive or curative strategies for egg allergy remains strongly warranted. Pilot studies have suggested that oral immunotherapy (IT) with raw or cooked preparations of egg may represent a safe alternative, immediately available to allergic subjects, but remains applicable to only nonanaphylactic patients. Due to the limitations of conventional IT, novel forms of immunotherapy are sought based on information obtained from the molecular characterization of major egg allergens. In the past decade, promising approaches to the treatment and prevention of egg allergy have been explored and include, among others, the production of hypoallergenic recombinant egg proteins, the development of customized peptides, and bacterial-mediated immunotherapy. Nonspecific approaches have also been evaluated, and preliminary trials with the use of probiotic bacteria have yielded encouraging results. The current understanding of egg allergens offers novel approaches toward the making of food products safe for human consumption and the development of efficient immunotherapeutic strategies.

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“…Moreover, using this method, the enzyme turnover can be monitored continuously. The assay times are short (1.5 h vs. 8 h) 14,15 and the detection limit is better than that reported in the literature 13,17 (0.5 ng ml 21 ). In addition, this assay is versatile enough to be used in different matrices with little or no preparation of some matrices.…”

Section: Discussionmentioning

confidence: 63%

“…12 It is also present in some vaccines 13 and is often used as a model for allergy studies and as a simulant for the protein toxin ricin. Ovalbumin in food and vaccines has been measured by immunoblotting, 12,14,15 double antibody well ELISA, 13,14 competitive immunoassay and electrophoresis. 15 These methods are time consuming, in some cases requiring overnight incubation.…”

Section: Introductionmentioning

confidence: 99%

Small volume bead assay for ovalbumin with electrochemical detection

Purushothama

Kradtap

Wijayawardhana

et al. 2001

Analyst

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A bead based sandwich enzyme immunoassay coupled to electrochemical detection for ovalbumin has been developed. The enzyme label alkaline phosphatase was used to convert the substrate 4-aminophenyl phosphate to electroactive product 4-aminophenol. The detection was done in a microdrop by continuously monitoring the enzyme turnover with a rotating disk electrode. This reduces dilution of the enzyme product, a key to achieving low detection limits. The assay developed has a detection limit of 0.1 ng ml-1. Assay sensitivity in complex matrices such as food and serum was compared.

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Immunochemical Identification and Quantification of Ovalbumin Additive in Canned Mushrooms

Cited by 22 publications

References 18 publications

Structure of Native and Heat‐denatured Ovalbumin as Revealed by Monoclonal Antibodies: Epitopic Changes during Heat Treatment

Structure of Native and Heat‐denatured Ovalbumin as Revealed by Monoclonal Antibodies: Epitopic Changes during Heat Treatment

Recent Advances in the Understanding of Egg Allergens: Basic, Industrial, and Clinical Perspectives

Small volume bead assay for ovalbumin with electrochemical detection

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