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

Authorized Users Only
2007
Authors
Polović, Natalija
Blanuša, Milan
Gavrović-Jankulović, Marija
Atanasković-Marković, Marina
Burazer, Lidija
Jankov, Ratko
Veličković, Tanja
Article (Published version)
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Abstract
Background: It is a general belief that a food allergen should be stable to gastric digestion. Various acidic plant polysaccharides, including pectin, are ubiquitous in fruit matrixes and can form hydrogels under low-pH conditions. Objective: The purpose of this study was to investigate the effect of hydrogel forming polysaccharide-rich fruit matrixes on in vivo gastric and in vitro pepsic digestion of fruit allergens. Methods: Fruit extract proteins (kiwi, banana, apple and cherry) and a purified major kiwi allergen Act c 2 were digested with simulated gastric fluid in accordance with the US Pharmacopeia. In vivo experiments on kiwi fruit digestion were performed on four healthy non-atopic volunteers by examining the gastric content 1 h after ingestion of kiwi fruit. The Act c 2 and kiwi proteins were detected in immunoblots using monoclonal anti-Act c 2 antibodies and rabbit polyclonal antisera. Results: Crude fruit extracts were resistant to digestion by pepsin when compared with co...mmonly prepared extracts. In the gastric content of all volunteers, following kiwi fruit ingestion and immunoblotting, intact Act c 2 was detected with anti-Act c 2 monoclonal antibodies, while kiwi proteins of higher molecular weights were detected using rabbit polyclonal antisera. Addition of apple fruit pectin (1.5% and 3%) to the purified kiwi allergen was able to protect it from pepsin digestion in vitro. Conclusion: The matrix effect in pectin-rich fruits can influence the digestibility of food proteins and thereby the process of allergic sensitization in atopic individuals.

Keywords:
Act c 2 / Digestibility assay / Food allergy / Matrix effect / Pectin / Thaumatin-like protein
Source:
Clinical and Experimental Allergy, 2007, 37, 5, 764-771
Funding / projects:
  • Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima (RS-142020)

DOI: 10.1111/j.1365-2222.2007.02703.x

ISSN: 0954-7894

PubMed: 17456224

WoS: 000245939700016

Scopus: 2-s2.0-34247376603
[ Google Scholar ]
55
45
URI
http://intor.torlakinstitut.com/handle/123456789/225
Collections
  • Radovi istraživača / Researchers’ publications
Institution/Community
Torlak
TY  - JOUR
AU  - Polović, Natalija
AU  - Blanuša, Milan
AU  - Gavrović-Jankulović, Marija
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija
AU  - Jankov, Ratko
AU  - Veličković, Tanja
PY  - 2007
UR  - http://intor.torlakinstitut.com/handle/123456789/225
AB  - Background: It is a general belief that a food allergen should be stable to gastric digestion. Various acidic plant polysaccharides, including pectin, are ubiquitous in fruit matrixes and can form hydrogels under low-pH conditions. Objective: The purpose of this study was to investigate the effect of hydrogel forming polysaccharide-rich fruit matrixes on in vivo gastric and in vitro pepsic digestion of fruit allergens. Methods: Fruit extract proteins (kiwi, banana, apple and cherry) and a purified major kiwi allergen Act c 2 were digested with simulated gastric fluid in accordance with the US Pharmacopeia. In vivo experiments on kiwi fruit digestion were performed on four healthy non-atopic volunteers by examining the gastric content 1 h after ingestion of kiwi fruit. The Act c 2 and kiwi proteins were detected in immunoblots using monoclonal anti-Act c 2 antibodies and rabbit polyclonal antisera. Results: Crude fruit extracts were resistant to digestion by pepsin when compared with commonly prepared extracts. In the gastric content of all volunteers, following kiwi fruit ingestion and immunoblotting, intact Act c 2 was detected with anti-Act c 2 monoclonal antibodies, while kiwi proteins of higher molecular weights were detected using rabbit polyclonal antisera. Addition of apple fruit pectin (1.5% and 3%) to the purified kiwi allergen was able to protect it from pepsin digestion in vitro. Conclusion: The matrix effect in pectin-rich fruits can influence the digestibility of food proteins and thereby the process of allergic sensitization in atopic individuals.
T2  - Clinical and Experimental Allergy
T1  - A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro
EP  - 771
IS  - 5
SP  - 764
VL  - 37
DO  - 10.1111/j.1365-2222.2007.02703.x
ER  - 
@article{
author = "Polović, Natalija and Blanuša, Milan and Gavrović-Jankulović, Marija and Atanasković-Marković, Marina and Burazer, Lidija and Jankov, Ratko and Veličković, Tanja",
year = "2007",
abstract = "Background: It is a general belief that a food allergen should be stable to gastric digestion. Various acidic plant polysaccharides, including pectin, are ubiquitous in fruit matrixes and can form hydrogels under low-pH conditions. Objective: The purpose of this study was to investigate the effect of hydrogel forming polysaccharide-rich fruit matrixes on in vivo gastric and in vitro pepsic digestion of fruit allergens. Methods: Fruit extract proteins (kiwi, banana, apple and cherry) and a purified major kiwi allergen Act c 2 were digested with simulated gastric fluid in accordance with the US Pharmacopeia. In vivo experiments on kiwi fruit digestion were performed on four healthy non-atopic volunteers by examining the gastric content 1 h after ingestion of kiwi fruit. The Act c 2 and kiwi proteins were detected in immunoblots using monoclonal anti-Act c 2 antibodies and rabbit polyclonal antisera. Results: Crude fruit extracts were resistant to digestion by pepsin when compared with commonly prepared extracts. In the gastric content of all volunteers, following kiwi fruit ingestion and immunoblotting, intact Act c 2 was detected with anti-Act c 2 monoclonal antibodies, while kiwi proteins of higher molecular weights were detected using rabbit polyclonal antisera. Addition of apple fruit pectin (1.5% and 3%) to the purified kiwi allergen was able to protect it from pepsin digestion in vitro. Conclusion: The matrix effect in pectin-rich fruits can influence the digestibility of food proteins and thereby the process of allergic sensitization in atopic individuals.",
journal = "Clinical and Experimental Allergy",
title = "A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro",
pages = "771-764",
number = "5",
volume = "37",
doi = "10.1111/j.1365-2222.2007.02703.x"
}
Polović, N., Blanuša, M., Gavrović-Jankulović, M., Atanasković-Marković, M., Burazer, L., Jankov, R.,& Veličković, T.. (2007). A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro. in Clinical and Experimental Allergy, 37(5), 764-771.
https://doi.org/10.1111/j.1365-2222.2007.02703.x
Polović N, Blanuša M, Gavrović-Jankulović M, Atanasković-Marković M, Burazer L, Jankov R, Veličković T. A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro. in Clinical and Experimental Allergy. 2007;37(5):764-771.
doi:10.1111/j.1365-2222.2007.02703.x .
Polović, Natalija, Blanuša, Milan, Gavrović-Jankulović, Marija, Atanasković-Marković, Marina, Burazer, Lidija, Jankov, Ratko, Veličković, Tanja, "A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro" in Clinical and Experimental Allergy, 37, no. 5 (2007):764-771,
https://doi.org/10.1111/j.1365-2222.2007.02703.x . .

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