TY  - CONF
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Ćirković Veličković, Tanja
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/887
AB  - A bottom-up proteomic study, using high-resolution tandem mass spectrometry (HRMS) and, PEAKS Studio X+ was performed to investigate the impact of peanut roasting on readily soluble allergens and their post-translational modification (PTM) profiles. Among four major peanut allergen groups, we found that Ara h 3 prevails in raw peanut extract (PE), similar to Ara h 1, while the opposite is true for Ara h 6, which is enriched in roasted PE; Ara h 2 bands are near the same intensity. HRMS detected more than 40 different types of modification in raw and roasted samples. Distinct variations in the types and occurrence of specific amino acid PTMs were identified between allergens present in raw and roasted samples. Roasting affected the most frequent modifications by enrichment of OxM, HyP, carbamoylation (KR), and deamidation. The PTMs could also be mapped to the regions of IgE-binding epitopes of Ara h 1–3 and Ara h 6. As porcine trypsin is used for HRMS sample preparation and is also a digestive protease, hindrance effects to trypsin efficacy regarding PTMs was assessed. Roasting caused dihydroxylation and formylation PTMs with hindrance effects to trypsin efficacy, while methylation on several K/R showed opposite effects. In the case of methylated R342, results suggested facilitation of tryptic performance at modified residue compared to unmodified counterpart, while in the rest of seven genuine sequences containing modified residues, trend was opposite. Further exploration of how different PTMs could affect digestion efficiencies of major gastric and intestinal peptidases is currently in works and a much-needed assessment to better understand the role of PTMs.
PB  - Faculty of Chemistry, Serbian Biochemical Society
C3  - Serbian Biochemical Society, Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia “Biochemistry in Biotechnology”
T1  - Mass spectrometry analysis reveals impact of peanut roasting on post-translational modifications of key allergens and their hinderence of trypsin digestion
EP  - 147
SP  - 146
ER  - 

@conference{
author = "Đukić, Teodora and Smiljanić, Katarina and Prodić, Ivana and Ćirković Veličković, Tanja",
year = "2023",
abstract = "A bottom-up proteomic study, using high-resolution tandem mass spectrometry (HRMS) and, PEAKS Studio X+ was performed to investigate the impact of peanut roasting on readily soluble allergens and their post-translational modification (PTM) profiles. Among four major peanut allergen groups, we found that Ara h 3 prevails in raw peanut extract (PE), similar to Ara h 1, while the opposite is true for Ara h 6, which is enriched in roasted PE; Ara h 2 bands are near the same intensity. HRMS detected more than 40 different types of modification in raw and roasted samples. Distinct variations in the types and occurrence of specific amino acid PTMs were identified between allergens present in raw and roasted samples. Roasting affected the most frequent modifications by enrichment of OxM, HyP, carbamoylation (KR), and deamidation. The PTMs could also be mapped to the regions of IgE-binding epitopes of Ara h 1–3 and Ara h 6. As porcine trypsin is used for HRMS sample preparation and is also a digestive protease, hindrance effects to trypsin efficacy regarding PTMs was assessed. Roasting caused dihydroxylation and formylation PTMs with hindrance effects to trypsin efficacy, while methylation on several K/R showed opposite effects. In the case of methylated R342, results suggested facilitation of tryptic performance at modified residue compared to unmodified counterpart, while in the rest of seven genuine sequences containing modified residues, trend was opposite. Further exploration of how different PTMs could affect digestion efficiencies of major gastric and intestinal peptidases is currently in works and a much-needed assessment to better understand the role of PTMs.",
publisher = "Faculty of Chemistry, Serbian Biochemical Society",
journal = "Serbian Biochemical Society, Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia “Biochemistry in Biotechnology”",
title = "Mass spectrometry analysis reveals impact of peanut roasting on post-translational modifications of key allergens and their hinderence of trypsin digestion",
pages = "147-146"
}

Đukić, T., Smiljanić, K., Prodić, I.,& Ćirković Veličković, T.. (2023). Mass spectrometry analysis reveals impact of peanut roasting on post-translational modifications of key allergens and their hinderence of trypsin digestion. in Serbian Biochemical Society, Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia “Biochemistry in Biotechnology”
Faculty of Chemistry, Serbian Biochemical Society., 146-147.

Đukić T, Smiljanić K, Prodić I, Ćirković Veličković T. Mass spectrometry analysis reveals impact of peanut roasting on post-translational modifications of key allergens and their hinderence of trypsin digestion. in Serbian Biochemical Society, Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia “Biochemistry in Biotechnology”. 2023;:146-147..

Đukić, Teodora, Smiljanić, Katarina, Prodić, Ivana, Ćirković Veličković, Tanja, "Mass spectrometry analysis reveals impact of peanut roasting on post-translational modifications of key allergens and their hinderence of trypsin digestion" in Serbian Biochemical Society, Twelfth Conference, International scientific meeting, September 21-23, 2023, Belgrade, Serbia “Biochemistry in Biotechnology” (2023):146-147.

TY  - CONF
AU  - MIhilović, Jelena
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Liu, Shu-Hua
AU  - Epstein, Michelle M.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/769
AB  - Peanut allergy affects approximately up to 3 % of children and up to 2 % of the adult world population, causing reactions ranging from mild to severe. Major peanut allergens are well characterized but little is known about their post-translational modifications and even less is known about the influence of thermal treatment on their profile. Protein post-translational modification patterns may differ between raw and thermally treated peanuts, which could affect its functional properties, such as allergic potential. In this study we combined proteomic and immunological methods to characterize the modifications or proteoforms of four major peanut allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6 in raw and roasted peanut. Bottom-up high-resolution accurate mass spectrometry and a specialized proteomics software package to identify, map and compare modifications of major peanut allergens between differently treated peanut kernels. Modification-specific antibody western blot was used to confirm the presence of modifications on major allergens in both extracts. Twenty different post-translational modifications in four prominent peanut allergens (Ara h 1-3, 6) were identified, while twelve were quantitatively compared between raw and roasted peanuts by high-resolution mass spectrometry and a proprietary proteomics software. post-translational modification specific antibodies confirmed the presence of these modifications in western-blots of raw and roasted peanuts. This study initiates appreciation of modifications and thermal processing affecting food quality, and development of state-of-the-art methodology in the risk assessment of allergen contamination.
C3  - FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia
T1  - Comparative quantitative immunoproteomic study of raw and roasted peanut major allergen modifications
EP  - 27
SP  - 27
UR  - https://hdl.handle.net/21.15107/rcub_intor_769
ER  - 

@conference{
author = "MIhilović, Jelena and Đukić, Teodora and Smiljanić, Katarina and Apostolović, Danijela and Liu, Shu-Hua and Epstein, Michelle M. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Peanut allergy affects approximately up to 3 % of children and up to 2 % of the adult world population, causing reactions ranging from mild to severe. Major peanut allergens are well characterized but little is known about their post-translational modifications and even less is known about the influence of thermal treatment on their profile. Protein post-translational modification patterns may differ between raw and thermally treated peanuts, which could affect its functional properties, such as allergic potential. In this study we combined proteomic and immunological methods to characterize the modifications or proteoforms of four major peanut allergens - Ara h 1, Ara h 2, Ara h 3 and Ara h 6 in raw and roasted peanut. Bottom-up high-resolution accurate mass spectrometry and a specialized proteomics software package to identify, map and compare modifications of major peanut allergens between differently treated peanut kernels. Modification-specific antibody western blot was used to confirm the presence of modifications on major allergens in both extracts. Twenty different post-translational modifications in four prominent peanut allergens (Ara h 1-3, 6) were identified, while twelve were quantitatively compared between raw and roasted peanuts by high-resolution mass spectrometry and a proprietary proteomics software. post-translational modification specific antibodies confirmed the presence of these modifications in western-blots of raw and roasted peanuts. This study initiates appreciation of modifications and thermal processing affecting food quality, and development of state-of-the-art methodology in the risk assessment of allergen contamination.",
journal = "FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia",
title = "Comparative quantitative immunoproteomic study of raw and roasted peanut major allergen modifications",
pages = "27-27",
url = "https://hdl.handle.net/21.15107/rcub_intor_769"
}

MIhilović, J., Đukić, T., Smiljanić, K., Apostolović, D., Liu, S., Epstein, M. M.,& Ćirković-Veličković, T.. (2021). Comparative quantitative immunoproteomic study of raw and roasted peanut major allergen modifications. in FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia, 27-27.
https://hdl.handle.net/21.15107/rcub_intor_769

MIhilović J, Đukić T, Smiljanić K, Apostolović D, Liu S, Epstein MM, Ćirković-Veličković T. Comparative quantitative immunoproteomic study of raw and roasted peanut major allergen modifications. in FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia. 2021;:27-27.
https://hdl.handle.net/21.15107/rcub_intor_769 .

MIhilović, Jelena, Đukić, Teodora, Smiljanić, Katarina, Apostolović, Danijela, Liu, Shu-Hua, Epstein, Michelle M., Ćirković-Veličković, Tanja, "Comparative quantitative immunoproteomic study of raw and roasted peanut major allergen modifications" in FoodEnTwin Symposium: Novel analytical approaches in food and environmental sciences, June 16-18, 2021 Belgrade, Serbia (2021):27-27,
https://hdl.handle.net/21.15107/rcub_intor_769 .