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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
Blanusa, M.
Gavrović-Jankulović, Marija
Atanasković-Marković, Marina
Burazer, Lidija M.
Jankov, Ratko M.
Ćirković-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 common...ly 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
Publisher:
  • Blackwell Publishing, Oxford
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 ]
53
45
URI
https://cherry.chem.bg.ac.rs/handle/123456789/827
Collections
  • Publikacije
Institution/Community
Hemijski fakultet
TY  - JOUR
AU  - Polović, Natalija
AU  - Blanusa, M.
AU  - Gavrović-Jankulović, Marija
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija M.
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/827
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.
PB  - Blackwell Publishing, Oxford
T2  - Clinical and Experimental Allergy
T1  - A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro
VL  - 37
IS  - 5
SP  - 764
EP  - 771
DO  - 10.1111/j.1365-2222.2007.02703.x
UR  - Kon_1780
ER  - 
@article{
author = "Polović, Natalija and Blanusa, M. and Gavrović-Jankulović, Marija and Atanasković-Marković, Marina and Burazer, Lidija M. and Jankov, Ratko M. and Ćirković-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.",
publisher = "Blackwell Publishing, Oxford",
journal = "Clinical and Experimental Allergy",
title = "A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro",
volume = "37",
number = "5",
pages = "764-771",
doi = "10.1111/j.1365-2222.2007.02703.x",
url = "Kon_1780"
}
Polović, N., Blanusa, M., Gavrović-Jankulović, M., Atanasković-Marković, M., Burazer, L. M., Jankov, R. M.,& Ćirković-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
Blackwell Publishing, Oxford., 37(5), 764-771.
https://doi.org/10.1111/j.1365-2222.2007.02703.x
Kon_1780
Polović N, Blanusa M, Gavrović-Jankulović M, Atanasković-Marković M, Burazer LM, Jankov RM, Ćirković-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
Kon_1780 .
Polović, Natalija, Blanusa, M., Gavrović-Jankulović, Marija, Atanasković-Marković, Marina, Burazer, Lidija M., Jankov, Ratko M., Ćirković-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 .,
Kon_1780 .

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