A matrix effect in pectin‐rich fruits hampers digestion of allergen by pepsin <i>in vivo</i> and <i>in vitro</i>

Polović, Natalija; Blanusa, Milan; Gavrović-Jankulović, Marija; Atanasković-Marković, Marina; Burazer, Lidija; Jankov, Ratko M.; Veličković, Tanja Ćirković

doi:10.1111/j.1365-2222.2007.02703.x

Cited by 67 publications

(45 citation statements)

References 39 publications

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“…TLPs were important constituents of the analyzed kiwifruit extracts representing 27 -31% of total proteins. TLPs abundance in the fruits together with the structural features (eight conserved disulphide bridges), and the complex plant-specific tissue matrix [38,39] may contribute to their survival in the gastrointestinal tract and the process of allergic sensitization. This is the first mAb-based sandwich ELISA developed for the quantification of the kiwi TLP allergen.…”

Section: Discussionmentioning

confidence: 99%

Quantification of the thaumatin‐like kiwi allergen by a monoclonal antibody‐based ELISA

Gavrović-Jankulović¹,

Spasic

Veličković

et al. 2008

Molecular Nutrition Food Res

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Thaumatin-like proteins (TLPs) have been established as a new family of fruit and pollen allergens. The aim of this study was to develop a two-site ELISA for the quantification of the thaumatin-like kiwi allergen (Act d 2) in kiwifruit extracts and kiwifruit-containing food products. Genomic DNA (gDNA) of Act d 2 was amplified and the deduced amino acid sequence was determined to obtain a primary structure. Act d 2 purified from kiwifruit extract by HPLC was identified by Edman degradation and MS. Balb/c mice were immunized with Act d 2 for the production of mAbs by hybridoma technology. The optimized ELISA measured Act d 2 concentrations ranging from 0.2 to 9.0 ng/mL, with intra- and interassay coefficients of variation of 3.65 and 10.44%, respectively. The developed ELISA is a useful method for the quantification of the thaumatin-like kiwi allergen in kiwifruit extracts as well as the allergen level in kiwifruit-containing food products. It may be a helpful analytical tool for the evaluation of the stability (integrity) of fruit allergen extracts for in vitro diagnosis.

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Section: Discussionmentioning

confidence: 99%

Quantification of the thaumatin‐like kiwi allergen by a monoclonal antibody‐based ELISA

Gavrović-Jankulović¹,

Spasic

Veličković

et al. 2008

Molecular Nutrition Food Res

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“…Thus, the food matrix may contain substances able to hamper enzymatic digestion by making physical obstacles to enzyme action. Those described so far are lipids, e.g., phosphatidylcholine [8,24] secreted in the stomach and also abundant in milk, as well as polysaccharides, e.g., pectin in fruit matrices [28,29].…”

Section: Introductionmentioning

confidence: 99%

“…When the digestibility of kiwi, banana, apple, and sour cherry TLPs were compared in vitro, kiwi TLP was the only gastric labile protein, being readily digested by pepsin within several minutes [28].…”

Section: Introductionmentioning

confidence: 99%

In Vivo Digestion of a Thaumatin-Like Kiwifruit Protein in Rats

et al. 2010

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Food allergens must exhibit sufficient gastrointestinal stability to reach the intestinal mucosa where absorption and sensitization can occur. Therefore, investigation of protein stability within the gastrointestinal tract may provide a prospective test for the allergenic potential of novel proteins. The aim of this work was to examine the effect of the fruit matrix and purified pectin on the digestion in vivo of kiwifruit allergens in the rat gastrointestinal system. The major kiwi allergen, Act d 2, was quantified in several compartments of the gastrointestinal tract by a monoclonal antibody-based ELISA. Protein intactness was demonstrated by immunoblot. Under conditions of complex food digestion in vivo, a pepsin-labile protein survived passage from the stomach to the caecum during a 3-h period. Decay of Act d 2 in the rat gut exhibited an exponential pattern. Ingestion of kiwifruit was followed by a decrease in both total and specific pepsin activity. When purified, Act d 2 allergen was consumed together with pure apple pectin; both gastric acidity as well as specific and total pepsin activity declined and thus protected 23% of the ingested allergen from digestion for 90 min. In conclusion, ingestion of pectin-rich fruits and particularly pectin

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“…The immunoreactivity of hydrolysis products in dialysates was considerably reduced by polysaccharides. Polovic et al (Polovic et al, 2007) demonstrated that addition of apple fruit pectin (1.5% and 3%) to the purified kiwi allergen Act c 2 was able to protect it from pepsin digestion in vitro. In vivo experiments on healthy non-atopic volunteers have shown that 1 h after ingestion of kiwi fruit in gastric content intact Act c 2 was still present.…”

Section: Noncovalent Modificationsmentioning

confidence: 99%

Enzymatic and Chemical Modifications of Food Allergens

Stanić-Vučinić¹,

Veličković²

2012

Allergic Diseases - Highlights in the Clinic, Mechanisms and Treatment

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A matrix effect in pectin‐rich fruits hampers digestion of allergen by pepsin in vivo and in vitro

Abstract: The matrix effect in pectin-rich fruits can influence the digestibility of food proteins and thereby the process of allergic sensitization in atopic individuals.

Cited by 67 publications

References 39 publications

Quantification of the thaumatin‐like kiwi allergen by a monoclonal antibody‐based ELISA

Quantification of the thaumatin‐like kiwi allergen by a monoclonal antibody‐based ELISA

In Vivo Digestion of a Thaumatin-Like Kiwifruit Protein in Rats

Enzymatic and Chemical Modifications of Food Allergens

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