A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro
Само за регистроване кориснике
2007
Аутори
Polović, NatalijaBlanusa, M.
Gavrović-Jankulović, Marija
Atanasković-Marković, Marina
Burazer, Lidija M.
Jankov, Ratko M.
Ćirković-Veličković, Tanja
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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.
Кључне речи:
Act c 2 / digestibility assay / food allergy / matrix effect / pectin / thaumatin-like proteinИзвор:
Clinical and Experimental Allergy, 2007, 37, 5, 764-771Издавач:
- Blackwell Publishing, Oxford
Финансирање / пројекти:
- Испитивање структуре и функције биолошки важних макромолекула у физиолошким и патолошким стањима (RS-MESTD-MPN2006-2010-142020)
DOI: 10.1111/j.1365-2222.2007.02703.x
ISSN: 0954-7894
PubMed: 17456224
WoS: 000245939700016
Scopus: 2-s2.0-34247376603
Колекције
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - 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 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" }
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
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 .
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 . .