TY  - JOUR
AU  - Khulal, Urmila
AU  - Stojadinović, Marija M.
AU  - Prodić, Ivana
AU  - Rajković, Andrea
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/766
AB  - The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.
PB  - Elsevier
T2  - Food Chemistry
T1  - Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix
SP  - 134981
VL  - 405
DO  - 10.1016/j.foodchem.2022.134981
ER  - 

@article{
author = "Khulal, Urmila and Stojadinović, Marija M. and Prodić, Ivana and Rajković, Andrea and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix",
pages = "134981",
volume = "405",
doi = "10.1016/j.foodchem.2022.134981"
}

Khulal, U., Stojadinović, M. M., Prodić, I., Rajković, A.,& Ćirković-Veličković, T.. (2023). Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry
Elsevier., 405, 134981.
https://doi.org/10.1016/j.foodchem.2022.134981

Khulal U, Stojadinović MM, Prodić I, Rajković A, Ćirković-Veličković T. Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry. 2023;405:134981.
doi:10.1016/j.foodchem.2022.134981 .

Khulal, Urmila, Stojadinović, Marija M., Prodić, Ivana, Rajković, Andrea, Ćirković-Veličković, Tanja, "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix" in Food Chemistry, 405 (2023):134981,
https://doi.org/10.1016/j.foodchem.2022.134981 . .

TY  - JOUR
AU  - Khulal, Urmila
AU  - Stojadinović, Marija M.
AU  - Prodić, Ivana
AU  - Rajković, Andrea
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://intor.torlakinstitut.com/handle/123456789/767
AB  - The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.
PB  - Elsevier
T2  - Food Chemistry
T1  - Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix
SP  - 134981
VL  - 405
UR  - https://hdl.handle.net/21.15107/rcub_intor_767
ER  - 

@article{
author = "Khulal, Urmila and Stojadinović, Marija M. and Prodić, Ivana and Rajković, Andrea and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix",
pages = "134981",
volume = "405",
url = "https://hdl.handle.net/21.15107/rcub_intor_767"
}

Khulal, U., Stojadinović, M. M., Prodić, I., Rajković, A.,& Ćirković-Veličković, T.. (2023). Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry
Elsevier., 405, 134981.
https://hdl.handle.net/21.15107/rcub_intor_767

Khulal U, Stojadinović MM, Prodić I, Rajković A, Ćirković-Veličković T. Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry. 2023;405:134981.
https://hdl.handle.net/21.15107/rcub_intor_767 .

Khulal, Urmila, Stojadinović, Marija M., Prodić, Ivana, Rajković, Andrea, Ćirković-Veličković, Tanja, "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix" in Food Chemistry, 405 (2023):134981,
https://hdl.handle.net/21.15107/rcub_intor_767 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Khulal, Urmila
AU  - Mutić, Jelena
AU  - Mihailović, Jelena
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/774
AB  - Objective: Haliotis discus (Japanese abalone), mollusks among various shellfish, is a highlynutritive food resource in the world, but also among the eight allergic food groups accounting forapproximately 90% of all immunoglobulin E food allergies worldwide. The general objective of ourresearch is to comprehensively investigate stability and structures of pepsin-resistant allergens, oftheir larger fragments, and of short digestion resistant peptides (SDRPs) released by pepsindigestion of whole raw and extract of shellfish, under standardized and physiologically relevantgastric conditions.Materials and Methods: Extract of raw whole shellfish (eRSS) and whole raw shellfish (wRSS),were pepsin digested according to standardized static digestion protocol. Controls were treated in asame manner without adding pepsin. Supernatant of samples and its counterpart controls wereprecipitated with TCA/acetone. Obtained proteins were assessed by 2D SDS PAGE and 1D SDS-PAGE, under reducing and non-reducing conditions. 1D SDS-PAGE of RSS were analyzed byncLC-MS/MS (Orbitrap LTQ) shot-gun proteomics. Relative quantification was performed by LFQalgorithm within Peaks 8.5 software package Bioinformatics Solutions Inc. (BSI), Waterloo,Canada.Results and Conclusion: 1D SDS-PAGE analysis of eRSS and wRSS, and its controls showed arange of proteins in varied concentrations between 10-250 kDa. In extracted and whole rawshellfish, approximately 22 prominent protein bands were observed including the distinct bandscorresponding with the molecular weights of recognized shellfish allergen, tropomyosin (37-39kDa). Fewer high molecular weight proteins were observed followed by protein smearing,specifically around the low molecular weight protein bands. The smearing could possibly be due tothe breakdown products and the glycation. There were slight differences between the proteinprofiles under reducing and non-reducing conditions as well. Nevertheless, there was the retentionof a band in the 37kDa molecular weight marker in all 4 samples, likely consistent with heat stabletropomyosin (TM). Mass spectrometry showed allergens that are characterized (Hal d 1 and Hal di1), with 90% of sequence homology with main tropomyosin allergens from seafood.Scientific impact and relevance: The results will highlight effects of food matrix on shellfishallergens digestibility proving its relevancy in molecular allergology. Moreover, an insight will beobtained on the differences in digestibility of allergenic versus non-allergenic tropomyosins in thereal food matrix.
PB  - Srpsko Udruženje za Proteomiku, SePA; IBISS
C3  - IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
T1  - Digestomics of Japanese abalone in real food matrix
EP  - 10
SP  - 10
UR  - https://hdl.handle.net/21.15107/rcub_intor_774
ER  - 

@conference{
author = "Prodić, Ivana and Khulal, Urmila and Mutić, Jelena and Mihailović, Jelena and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Objective: Haliotis discus (Japanese abalone), mollusks among various shellfish, is a highlynutritive food resource in the world, but also among the eight allergic food groups accounting forapproximately 90% of all immunoglobulin E food allergies worldwide. The general objective of ourresearch is to comprehensively investigate stability and structures of pepsin-resistant allergens, oftheir larger fragments, and of short digestion resistant peptides (SDRPs) released by pepsindigestion of whole raw and extract of shellfish, under standardized and physiologically relevantgastric conditions.Materials and Methods: Extract of raw whole shellfish (eRSS) and whole raw shellfish (wRSS),were pepsin digested according to standardized static digestion protocol. Controls were treated in asame manner without adding pepsin. Supernatant of samples and its counterpart controls wereprecipitated with TCA/acetone. Obtained proteins were assessed by 2D SDS PAGE and 1D SDS-PAGE, under reducing and non-reducing conditions. 1D SDS-PAGE of RSS were analyzed byncLC-MS/MS (Orbitrap LTQ) shot-gun proteomics. Relative quantification was performed by LFQalgorithm within Peaks 8.5 software package Bioinformatics Solutions Inc. (BSI), Waterloo,Canada.Results and Conclusion: 1D SDS-PAGE analysis of eRSS and wRSS, and its controls showed arange of proteins in varied concentrations between 10-250 kDa. In extracted and whole rawshellfish, approximately 22 prominent protein bands were observed including the distinct bandscorresponding with the molecular weights of recognized shellfish allergen, tropomyosin (37-39kDa). Fewer high molecular weight proteins were observed followed by protein smearing,specifically around the low molecular weight protein bands. The smearing could possibly be due tothe breakdown products and the glycation. There were slight differences between the proteinprofiles under reducing and non-reducing conditions as well. Nevertheless, there was the retentionof a band in the 37kDa molecular weight marker in all 4 samples, likely consistent with heat stabletropomyosin (TM). Mass spectrometry showed allergens that are characterized (Hal d 1 and Hal di1), with 90% of sequence homology with main tropomyosin allergens from seafood.Scientific impact and relevance: The results will highlight effects of food matrix on shellfishallergens digestibility proving its relevancy in molecular allergology. Moreover, an insight will beobtained on the differences in digestibility of allergenic versus non-allergenic tropomyosins in thereal food matrix.",
publisher = "Srpsko Udruženje za Proteomiku, SePA; IBISS",
journal = "IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija",
title = "Digestomics of Japanese abalone in real food matrix",
pages = "10-10",
url = "https://hdl.handle.net/21.15107/rcub_intor_774"
}

Prodić, I., Khulal, U., Mutić, J., Mihailović, J., Smiljanić, K.,& Ćirković-Veličković, T.. (2018). Digestomics of Japanese abalone in real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija
Srpsko Udruženje za Proteomiku, SePA; IBISS., 10-10.
https://hdl.handle.net/21.15107/rcub_intor_774

Prodić I, Khulal U, Mutić J, Mihailović J, Smiljanić K, Ćirković-Veličković T. Digestomics of Japanese abalone in real food matrix. in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija. 2018;:10-10.
https://hdl.handle.net/21.15107/rcub_intor_774 .

Prodić, Ivana, Khulal, Urmila, Mutić, Jelena, Mihailović, Jelena, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Digestomics of Japanese abalone in real food matrix" in IV Simpozijum srpskog udruženja za proteomiku – SePA, Interaktomika i glikoproteomika: novi pristup u analizi proteina na velikoj skali, 25. maj 2018, Beograd, Srbija (2018):10-10,
https://hdl.handle.net/21.15107/rcub_intor_774 .