TY  - JOUR
AU  - Tantoush, Ziyad
AU  - Apostolović, Danijela
AU  - Kravić, Bojana
AU  - Prodić, Ivana
AU  - Mihajlovic, Luka
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1311
AB  - The in vitro gastric digestion of several food allergens (beta-lactoglobulin (BLG), alpha-lactalbumin (LA) and peanut allergens (PE)) in the presence of a catechin-enriched polyphenol extract of green tea (GTC), oxidized polyphenols and phenol oxidase processed food allergens and GTC was investigated. Pepsin-resistant proteins, such as BLG, major peanut allergens, Ara h 1 and Ara h 2, degrade faster in the presence of catechin-enriched green tea polyphenols. Phenol oxidase polymerized GTC affected adversely protein digestion of BLG and LA, but not digestion of PE proteins. Protecting effect of polyphenols correlated well with the ability of proteins to form insoluble complexes with oxidized catechins. Cross-linking of proteins and polyphenols further extended the half-lives of BLG and LA in the in vitro digestion by pepsin. Catechin-enriched green tea polyphenols of food supplements facilitate pepsin digestion of major food allergens, but hamper their digestion if oxidized and polymerized by phenol oxidase. (c) 2012 Elsevier Ltd. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Functional Foods
T1  - Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase
VL  - 4
IS  - 3
SP  - 650
EP  - 660
DO  - 10.1016/j.jff.2012.04.006
ER  - 

@article{
author = "Tantoush, Ziyad and Apostolović, Danijela and Kravić, Bojana and Prodić, Ivana and Mihajlovic, Luka and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2012",
abstract = "The in vitro gastric digestion of several food allergens (beta-lactoglobulin (BLG), alpha-lactalbumin (LA) and peanut allergens (PE)) in the presence of a catechin-enriched polyphenol extract of green tea (GTC), oxidized polyphenols and phenol oxidase processed food allergens and GTC was investigated. Pepsin-resistant proteins, such as BLG, major peanut allergens, Ara h 1 and Ara h 2, degrade faster in the presence of catechin-enriched green tea polyphenols. Phenol oxidase polymerized GTC affected adversely protein digestion of BLG and LA, but not digestion of PE proteins. Protecting effect of polyphenols correlated well with the ability of proteins to form insoluble complexes with oxidized catechins. Cross-linking of proteins and polyphenols further extended the half-lives of BLG and LA in the in vitro digestion by pepsin. Catechin-enriched green tea polyphenols of food supplements facilitate pepsin digestion of major food allergens, but hamper their digestion if oxidized and polymerized by phenol oxidase. (c) 2012 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Functional Foods",
title = "Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase",
volume = "4",
number = "3",
pages = "650-660",
doi = "10.1016/j.jff.2012.04.006"
}

Tantoush, Z., Apostolović, D., Kravić, B., Prodić, I., Mihajlovic, L., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2012). Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase. in Journal of Functional Foods
Elsevier Science Bv, Amsterdam., 4(3), 650-660.
https://doi.org/10.1016/j.jff.2012.04.006

Tantoush Z, Apostolović D, Kravić B, Prodić I, Mihajlovic L, Stanić-Vučinić D, Ćirković-Veličković T. Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase. in Journal of Functional Foods. 2012;4(3):650-660.
doi:10.1016/j.jff.2012.04.006 .

Tantoush, Ziyad, Apostolović, Danijela, Kravić, Bojana, Prodić, Ivana, Mihajlovic, Luka, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Green tea catechins of food, supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase" in Journal of Functional Foods, 4, no. 3 (2012):650-660,
https://doi.org/10.1016/j.jff.2012.04.006 . .

TY  - JOUR
AU  - Tantoush, Ziyad
AU  - Stanić, Dragana
AU  - Stojadinović, Marija M.
AU  - Ognjenović, Jana
AU  - Mihajlovic, Luka
AU  - Atanasković-Marković, Marina
AU  - Ćirković-Veličković, Tanja
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1137
AB  - beta-Lactoglobulin (BLG) is an important nutrient of dairy products, but it represents a serious health risk in patients allergic to milk. Sour cherry (Prunus cerasus L) extract (SCE) is frequently added as a natural food colour in composite foods, such as fruit yogurt, ice creams, frappes and milkshakes. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an SCE and to characterise the obtained products for their bioactivity. Laccase cross-linked BLG in the presence of sour cherry phenolics. In a basophil-activation assay, the allergenicity of the cross-linked protein was shown to decrease in all nine cow's milk-allergic patients, while digestibility of the remaining monomeric BLG in simulated conditions of the gastrointestinal tract increased. Tryptic peptides became immediately available in BLG treated by laccase and laccase/SCE. The hydrolysates obtained by trypsin digestion of BLG/laccase/SCE showed an increase of 57% in radical-scavenging activity, compared to the control BLG. Enzymatic processing and usage of natural phenolic extracts as mediators of enzymatic reaction may improve BLG safety and the availability of peptides following digestion, while conserving its bioactivity.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics
VL  - 125
IS  - 1
SP  - 84
EP  - 91
DO  - 10.1016/j.foodchem.2010.08.040
ER  - 

@article{
author = "Tantoush, Ziyad and Stanić, Dragana and Stojadinović, Marija M. and Ognjenović, Jana and Mihajlovic, Luka and Atanasković-Marković, Marina and Ćirković-Veličković, Tanja",
year = "2011",
abstract = "beta-Lactoglobulin (BLG) is an important nutrient of dairy products, but it represents a serious health risk in patients allergic to milk. Sour cherry (Prunus cerasus L) extract (SCE) is frequently added as a natural food colour in composite foods, such as fruit yogurt, ice creams, frappes and milkshakes. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an SCE and to characterise the obtained products for their bioactivity. Laccase cross-linked BLG in the presence of sour cherry phenolics. In a basophil-activation assay, the allergenicity of the cross-linked protein was shown to decrease in all nine cow's milk-allergic patients, while digestibility of the remaining monomeric BLG in simulated conditions of the gastrointestinal tract increased. Tryptic peptides became immediately available in BLG treated by laccase and laccase/SCE. The hydrolysates obtained by trypsin digestion of BLG/laccase/SCE showed an increase of 57% in radical-scavenging activity, compared to the control BLG. Enzymatic processing and usage of natural phenolic extracts as mediators of enzymatic reaction may improve BLG safety and the availability of peptides following digestion, while conserving its bioactivity.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics",
volume = "125",
number = "1",
pages = "84-91",
doi = "10.1016/j.foodchem.2010.08.040"
}

Tantoush, Z., Stanić, D., Stojadinović, M. M., Ognjenović, J., Mihajlovic, L., Atanasković-Marković, M.,& Ćirković-Veličković, T.. (2011). Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics. in Food Chemistry
Elsevier Sci Ltd, Oxford., 125(1), 84-91.
https://doi.org/10.1016/j.foodchem.2010.08.040

Tantoush Z, Stanić D, Stojadinović MM, Ognjenović J, Mihajlovic L, Atanasković-Marković M, Ćirković-Veličković T. Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics. in Food Chemistry. 2011;125(1):84-91.
doi:10.1016/j.foodchem.2010.08.040 .

Tantoush, Ziyad, Stanić, Dragana, Stojadinović, Marija M., Ognjenović, Jana, Mihajlovic, Luka, Atanasković-Marković, Marina, Ćirković-Veličković, Tanja, "Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics" in Food Chemistry, 125, no. 1 (2011):84-91,
https://doi.org/10.1016/j.foodchem.2010.08.040 . .

TY  - JOUR
AU  - Tantoush, Ziyad
AU  - Mihajlovic, Luka
AU  - Kravić, Bojana
AU  - Ognjenović, Jana
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1174
AB  - beta-Lactoglobulin (BLG) is an important nutrient of dairy products and an important allergen in cow's milk allergy. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an apple phenolic extract (APE) and to characterize the obtained products for their digestibility by pepsin and pancreatin. The composition of the apple phenolics used for cross-linking was determined by liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS). The apple phenolic extract contained significant amounts of quercetin glycosides, catechins and chlorogenic acid. The laccase cross-linked BLG in the presence of apple phenolics. The polymerization rendered the protein insoluble in the reaction mixture. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the cross-linking reaction mixture revealed a heterogeneous mixture of high molecular masses (cross-linked BLG), with a fraction of the BLG remaining monomeric. Enzymatic processing of BLG by laccase and apple polyphenols as mediators can decrease the biphasal pepsin pancreatin digestibility of the monomeric and cross-linked protein, thus decreasing its nutritional value. In addition, reduced BLG digestibility can decrease its allergenic potential. Apple polyphenols can find usage in the creation of new, more functional food products, designed to prevent obesity and hypersensitivity-related disorders.
AB  - β-Laktoglobulin (BLG) je važan nutrijent mlečnih proizvoda i važan alergen kod alergija na kravlje mleko. Cilj ove studije je bilo ispitivanje potencijala lakaze da unakrsno poveže BLG u prisustvu fenolnog ekstrakta jabuke (APE), kao i karakterizacija dobijenih proizvoda sa aspekta njihove digestibilnosti pepsinom i pankreatinom. Kompozicija fenola jabuke korišćenih za unakrsno povezivanje određena je pomoću LC-ESI-MS. Fenolni ekstrakt jabuke sadrži znatne količine glikozida kvercetina, katehine i hlorogensku kiselinu. BLG je unakrsno povezan lakazom u prisustvu fenola jabuke, pri čemu je polimerizacija učinila BLG nerastvornim u reakcionoj smeši. SDS-PAGE analiza pokazala je da reakciona smeša sadrži heterogenu smešu velikih molekulskih masa (unakrsno povezan BLG), kao i deo zaostalog monomernog BLG. Enzimsko procesovanje BLG lakazom, u prisustvu polifenola jabuke kao medijatora, može smanjiti bifaznu pepsin-pankreatinsku digestibilnost kako monomernog, tako i unakrsno povezanog BLG, i na taj način smanjiti njegovu nutritivnu vrednost. Takođe, smanjena digestibilnost BLG može smanjiti njegov alergeni potencijal. Polifenoli jabuke mogu se koristiti za kreiranje novih, funkcionalnijih prehrambenih proizvoda, dizajniranih za prevenciju kako gojaznosti, tako i bolesti vezanih za preosetljivost.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Digestibility of beta-lactoglobulin following cross-linking by Trametes versicolor laccase and apple polyphenols
T1  - Digestibilnost β-laktoglobulina nakon njegovog unakrsnog povezivanja dejstvom lakaze iz Trametes versicolor i polifenola iz jabuke
VL  - 76
IS  - 6
SP  - 847
EP  - 855
DO  - 10.2298/JSC101201077T
ER  - 

@article{
author = "Tantoush, Ziyad and Mihajlovic, Luka and Kravić, Bojana and Ognjenović, Jana and Jankov, Ratko M. and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2011",
abstract = "beta-Lactoglobulin (BLG) is an important nutrient of dairy products and an important allergen in cow's milk allergy. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an apple phenolic extract (APE) and to characterize the obtained products for their digestibility by pepsin and pancreatin. The composition of the apple phenolics used for cross-linking was determined by liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS). The apple phenolic extract contained significant amounts of quercetin glycosides, catechins and chlorogenic acid. The laccase cross-linked BLG in the presence of apple phenolics. The polymerization rendered the protein insoluble in the reaction mixture. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the cross-linking reaction mixture revealed a heterogeneous mixture of high molecular masses (cross-linked BLG), with a fraction of the BLG remaining monomeric. Enzymatic processing of BLG by laccase and apple polyphenols as mediators can decrease the biphasal pepsin pancreatin digestibility of the monomeric and cross-linked protein, thus decreasing its nutritional value. In addition, reduced BLG digestibility can decrease its allergenic potential. Apple polyphenols can find usage in the creation of new, more functional food products, designed to prevent obesity and hypersensitivity-related disorders., β-Laktoglobulin (BLG) je važan nutrijent mlečnih proizvoda i važan alergen kod alergija na kravlje mleko. Cilj ove studije je bilo ispitivanje potencijala lakaze da unakrsno poveže BLG u prisustvu fenolnog ekstrakta jabuke (APE), kao i karakterizacija dobijenih proizvoda sa aspekta njihove digestibilnosti pepsinom i pankreatinom. Kompozicija fenola jabuke korišćenih za unakrsno povezivanje određena je pomoću LC-ESI-MS. Fenolni ekstrakt jabuke sadrži znatne količine glikozida kvercetina, katehine i hlorogensku kiselinu. BLG je unakrsno povezan lakazom u prisustvu fenola jabuke, pri čemu je polimerizacija učinila BLG nerastvornim u reakcionoj smeši. SDS-PAGE analiza pokazala je da reakciona smeša sadrži heterogenu smešu velikih molekulskih masa (unakrsno povezan BLG), kao i deo zaostalog monomernog BLG. Enzimsko procesovanje BLG lakazom, u prisustvu polifenola jabuke kao medijatora, može smanjiti bifaznu pepsin-pankreatinsku digestibilnost kako monomernog, tako i unakrsno povezanog BLG, i na taj način smanjiti njegovu nutritivnu vrednost. Takođe, smanjena digestibilnost BLG može smanjiti njegov alergeni potencijal. Polifenoli jabuke mogu se koristiti za kreiranje novih, funkcionalnijih prehrambenih proizvoda, dizajniranih za prevenciju kako gojaznosti, tako i bolesti vezanih za preosetljivost.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Digestibility of beta-lactoglobulin following cross-linking by Trametes versicolor laccase and apple polyphenols, Digestibilnost β-laktoglobulina nakon njegovog unakrsnog povezivanja dejstvom lakaze iz Trametes versicolor i polifenola iz jabuke",
volume = "76",
number = "6",
pages = "847-855",
doi = "10.2298/JSC101201077T"
}

Tantoush, Z., Mihajlovic, L., Kravić, B., Ognjenović, J., Jankov, R. M., Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2011). Digestibility of beta-lactoglobulin following cross-linking by Trametes versicolor laccase and apple polyphenols. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 76(6), 847-855.
https://doi.org/10.2298/JSC101201077T

Tantoush Z, Mihajlovic L, Kravić B, Ognjenović J, Jankov RM, Ćirković-Veličković T, Stanić-Vučinić D. Digestibility of beta-lactoglobulin following cross-linking by Trametes versicolor laccase and apple polyphenols. in Journal of the Serbian Chemical Society. 2011;76(6):847-855.
doi:10.2298/JSC101201077T .

Tantoush, Ziyad, Mihajlovic, Luka, Kravić, Bojana, Ognjenović, Jana, Jankov, Ratko M., Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "Digestibility of beta-lactoglobulin following cross-linking by Trametes versicolor laccase and apple polyphenols" in Journal of the Serbian Chemical Society, 76, no. 6 (2011):847-855,
https://doi.org/10.2298/JSC101201077T . .