TY  - JOUR
AU  - Wu, Xuli
AU  - He, Kan
AU  - Ćirković-Veličković, Tanja
AU  - Liu, Zhigang
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4621
AB  - Edible insects are a food source that has high nutritional value. Domestic silkworm pupae are an important by-product of sericulture and have a long history as food and feed ingredients in East Asia. Silkworm pupae are a good source of protein, lipids, minerals, and vitamins and are considered a good source of nutrients for humans. Silkworm pupae are a valuable insect source of substances used in healthcare products, medicines, food additives, and animal feed. Because silkworm pupae are being increasingly used in the human diet, potential allergic reactions to the substances they contain must be elucidated. Here, we present an overview of the benefits of silkworm pupae. First, we describe their nutritional value. Second, we report their functional properties and applications, focusing on their potential use in the food and pharmaceutical industries. Finally, we consider the current state of research regarding silkworm pupae-induced allergies.
PB  - Wiley
T2  - Food Science & Nutrition
T1  - Nutritional, functional, and allergenic properties of silkworm pupae
VL  - 9
IS  - 8
SP  - 4655
EP  - 4665
DO  - 10.1002/fsn3.2428
ER  - 

@article{
author = "Wu, Xuli and He, Kan and Ćirković-Veličković, Tanja and Liu, Zhigang",
year = "2021",
abstract = "Edible insects are a food source that has high nutritional value. Domestic silkworm pupae are an important by-product of sericulture and have a long history as food and feed ingredients in East Asia. Silkworm pupae are a good source of protein, lipids, minerals, and vitamins and are considered a good source of nutrients for humans. Silkworm pupae are a valuable insect source of substances used in healthcare products, medicines, food additives, and animal feed. Because silkworm pupae are being increasingly used in the human diet, potential allergic reactions to the substances they contain must be elucidated. Here, we present an overview of the benefits of silkworm pupae. First, we describe their nutritional value. Second, we report their functional properties and applications, focusing on their potential use in the food and pharmaceutical industries. Finally, we consider the current state of research regarding silkworm pupae-induced allergies.",
publisher = "Wiley",
journal = "Food Science & Nutrition",
title = "Nutritional, functional, and allergenic properties of silkworm pupae",
volume = "9",
number = "8",
pages = "4655-4665",
doi = "10.1002/fsn3.2428"
}

Wu, X., He, K., Ćirković-Veličković, T.,& Liu, Z.. (2021). Nutritional, functional, and allergenic properties of silkworm pupae. in Food Science & Nutrition
Wiley., 9(8), 4655-4665.
https://doi.org/10.1002/fsn3.2428

Wu X, He K, Ćirković-Veličković T, Liu Z. Nutritional, functional, and allergenic properties of silkworm pupae. in Food Science & Nutrition. 2021;9(8):4655-4665.
doi:10.1002/fsn3.2428 .

Wu, Xuli, He, Kan, Ćirković-Veličković, Tanja, Liu, Zhigang, "Nutritional, functional, and allergenic properties of silkworm pupae" in Food Science & Nutrition, 9, no. 8 (2021):4655-4665,
https://doi.org/10.1002/fsn3.2428 . .

TY  - JOUR
AU  - Zhang, Tingting
AU  - Hu, Zongyi
AU  - Cheng, Yongwei
AU  - Xu, Haoxie
AU  - Ćirković-Veličković, Tanja
AU  - He, Kan
AU  - Sun, Fan
AU  - He, Zhendan
AU  - Liu, Zhigang
AU  - Wu, Xuli
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3954
AB  - A previous study demonstrated decreased allergenicity in vitro of some food allergens after conjugation with polyphenols. However, little is known about how polyphenol conjugation with food allergens affects in vivo allergenicity. We conjugated a well-known food allergen, ovalbumin (OVA), with quercetin (QUE) to assess the potential allergenicity of OVA in vitro and in vivo in a BALB/c mouse model. QUE could covalently conjugate with OVA and changed the protein structure, which might destroy and/or mask OVA epitopes. Conjugation with QUE decreased IgE binding properties and the release capacity of the conjugated OVA. In vivo, as compared with native protein, conjugation with QUE decreased the levels of IgE, IgG1, IgG, plasma histamine, and mast cell protease-1 (mMCP-1) on the surface of sensitized mast cells, along with decreased FcϵRI+ and c-kit+ expression. The levels of Th2-related cytokines (IL-4, IL-5, IL-13) decreased and that of a Th1-related cytokine (IFN-Î) increased slightly, which suggests that conjugation with QUE modulated the imbalance of the Th1/Th2 immune response. Conjugation of OVA with QUE could reduce OVA allergenicity in vitro and in vivo, which could provide information for reducing food allergenicity by conjugation with polyphenols. Copyright © 2020 American Chemical Society.
PB  - American Chemical Society
T2  - Journal of Agricultural and Food Chemistry
T1  - Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin
VL  - 68
IS  - 13
SP  - 4027
EP  - 4035
DO  - 10.1021/acs.jafc.0c00461
ER  - 

@article{
author = "Zhang, Tingting and Hu, Zongyi and Cheng, Yongwei and Xu, Haoxie and Ćirković-Veličković, Tanja and He, Kan and Sun, Fan and He, Zhendan and Liu, Zhigang and Wu, Xuli",
year = "2020",
abstract = "A previous study demonstrated decreased allergenicity in vitro of some food allergens after conjugation with polyphenols. However, little is known about how polyphenol conjugation with food allergens affects in vivo allergenicity. We conjugated a well-known food allergen, ovalbumin (OVA), with quercetin (QUE) to assess the potential allergenicity of OVA in vitro and in vivo in a BALB/c mouse model. QUE could covalently conjugate with OVA and changed the protein structure, which might destroy and/or mask OVA epitopes. Conjugation with QUE decreased IgE binding properties and the release capacity of the conjugated OVA. In vivo, as compared with native protein, conjugation with QUE decreased the levels of IgE, IgG1, IgG, plasma histamine, and mast cell protease-1 (mMCP-1) on the surface of sensitized mast cells, along with decreased FcϵRI+ and c-kit+ expression. The levels of Th2-related cytokines (IL-4, IL-5, IL-13) decreased and that of a Th1-related cytokine (IFN-Î) increased slightly, which suggests that conjugation with QUE modulated the imbalance of the Th1/Th2 immune response. Conjugation of OVA with QUE could reduce OVA allergenicity in vitro and in vivo, which could provide information for reducing food allergenicity by conjugation with polyphenols. Copyright © 2020 American Chemical Society.",
publisher = "American Chemical Society",
journal = "Journal of Agricultural and Food Chemistry",
title = "Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin",
volume = "68",
number = "13",
pages = "4027-4035",
doi = "10.1021/acs.jafc.0c00461"
}

Zhang, T., Hu, Z., Cheng, Y., Xu, H., Ćirković-Veličković, T., He, K., Sun, F., He, Z., Liu, Z.,& Wu, X.. (2020). Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin. in Journal of Agricultural and Food Chemistry
American Chemical Society., 68(13), 4027-4035.
https://doi.org/10.1021/acs.jafc.0c00461

Zhang T, Hu Z, Cheng Y, Xu H, Ćirković-Veličković T, He K, Sun F, He Z, Liu Z, Wu X. Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin. in Journal of Agricultural and Food Chemistry. 2020;68(13):4027-4035.
doi:10.1021/acs.jafc.0c00461 .

Zhang, Tingting, Hu, Zongyi, Cheng, Yongwei, Xu, Haoxie, Ćirković-Veličković, Tanja, He, Kan, Sun, Fan, He, Zhendan, Liu, Zhigang, Wu, Xuli, "Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin" in Journal of Agricultural and Food Chemistry, 68, no. 13 (2020):4027-4035,
https://doi.org/10.1021/acs.jafc.0c00461 . .

TY  - JOUR
AU  - Zhang, Tingting
AU  - Hu, Zongyi
AU  - Cheng, Yongwei
AU  - Xu, Haoxie
AU  - Ćirković-Veličković, Tanja
AU  - He, Kan
AU  - Sun, Fan
AU  - He, Zhendan
AU  - Liu, Zhigang
AU  - Wu, Xuli
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3953
AB  - A previous study demonstrated decreased allergenicity in vitro of some food allergens after conjugation with polyphenols. However, little is known about how polyphenol conjugation with food allergens affects in vivo allergenicity. We conjugated a well-known food allergen, ovalbumin (OVA), with quercetin (QUE) to assess the potential allergenicity of OVA in vitro and in vivo in a BALB/c mouse model. QUE could covalently conjugate with OVA and changed the protein structure, which might destroy and/or mask OVA epitopes. Conjugation with QUE decreased IgE binding properties and the release capacity of the conjugated OVA. In vivo, as compared with native protein, conjugation with QUE decreased the levels of IgE, IgG1, IgG, plasma histamine, and mast cell protease-1 (mMCP-1) on the surface of sensitized mast cells, along with decreased FcϵRI+ and c-kit+ expression. The levels of Th2-related cytokines (IL-4, IL-5, IL-13) decreased and that of a Th1-related cytokine (IFN-Î) increased slightly, which suggests that conjugation with QUE modulated the imbalance of the Th1/Th2 immune response. Conjugation of OVA with QUE could reduce OVA allergenicity in vitro and in vivo, which could provide information for reducing food allergenicity by conjugation with polyphenols. Copyright © 2020 American Chemical Society.
PB  - American Chemical Society
T2  - Journal of Agricultural and Food Chemistry
T1  - Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin
VL  - 68
IS  - 13
SP  - 4027
EP  - 4035
DO  - 10.1021/acs.jafc.0c00461
ER  - 

@article{
author = "Zhang, Tingting and Hu, Zongyi and Cheng, Yongwei and Xu, Haoxie and Ćirković-Veličković, Tanja and He, Kan and Sun, Fan and He, Zhendan and Liu, Zhigang and Wu, Xuli",
year = "2020",
abstract = "A previous study demonstrated decreased allergenicity in vitro of some food allergens after conjugation with polyphenols. However, little is known about how polyphenol conjugation with food allergens affects in vivo allergenicity. We conjugated a well-known food allergen, ovalbumin (OVA), with quercetin (QUE) to assess the potential allergenicity of OVA in vitro and in vivo in a BALB/c mouse model. QUE could covalently conjugate with OVA and changed the protein structure, which might destroy and/or mask OVA epitopes. Conjugation with QUE decreased IgE binding properties and the release capacity of the conjugated OVA. In vivo, as compared with native protein, conjugation with QUE decreased the levels of IgE, IgG1, IgG, plasma histamine, and mast cell protease-1 (mMCP-1) on the surface of sensitized mast cells, along with decreased FcϵRI+ and c-kit+ expression. The levels of Th2-related cytokines (IL-4, IL-5, IL-13) decreased and that of a Th1-related cytokine (IFN-Î) increased slightly, which suggests that conjugation with QUE modulated the imbalance of the Th1/Th2 immune response. Conjugation of OVA with QUE could reduce OVA allergenicity in vitro and in vivo, which could provide information for reducing food allergenicity by conjugation with polyphenols. Copyright © 2020 American Chemical Society.",
publisher = "American Chemical Society",
journal = "Journal of Agricultural and Food Chemistry",
title = "Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin",
volume = "68",
number = "13",
pages = "4027-4035",
doi = "10.1021/acs.jafc.0c00461"
}

Zhang, T., Hu, Z., Cheng, Y., Xu, H., Ćirković-Veličković, T., He, K., Sun, F., He, Z., Liu, Z.,& Wu, X.. (2020). Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin. in Journal of Agricultural and Food Chemistry
American Chemical Society., 68(13), 4027-4035.
https://doi.org/10.1021/acs.jafc.0c00461

Zhang T, Hu Z, Cheng Y, Xu H, Ćirković-Veličković T, He K, Sun F, He Z, Liu Z, Wu X. Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin. in Journal of Agricultural and Food Chemistry. 2020;68(13):4027-4035.
doi:10.1021/acs.jafc.0c00461 .

Zhang, Tingting, Hu, Zongyi, Cheng, Yongwei, Xu, Haoxie, Ćirković-Veličković, Tanja, He, Kan, Sun, Fan, He, Zhendan, Liu, Zhigang, Wu, Xuli, "Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin" in Journal of Agricultural and Food Chemistry, 68, no. 13 (2020):4027-4035,
https://doi.org/10.1021/acs.jafc.0c00461 . .

TY  - JOUR
AU  - He, Weiyi
AU  - Zhang, Tingting
AU  - Ćirković-Veličković, Tanja
AU  - Li, Shuiming
AU  - Lyu, Yansi
AU  - Wang, Linlin
AU  - Yi, Jiang
AU  - Liu, Zhigang
AU  - He, Zhendan
AU  - Wu, Xuli
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4053
AB  - Ara h1 is a major allergen from peanut. We investigated the effect of covalent conjugation of Ara h1 and dietary polyphenols on allergenicity and functional properties of Ara h1. Enzyme-linked immunosorbent assay revealed that the covalent conjugation of dietary polyphenols significantly reduced the IgE binding capacity of Ara h1. Covalent binding of dietary polyphenols with Ara h1 reduced histamine release by 40% in basophils. The decreased IgE binding capacity of Ara h1 could be ascribed to changes in protein conformation. The IgE epitope of Ara h1 might be blocked by polyphenols at the binding site. Analysis of pepsin digestion of Ara h1–polyphenol conjugates indicated that the covalent binding increased pepsin digestibility and reduced IgE binding capacity. Furthermore, covalent conjugation of Ara h1 with polyphenols decreased denaturation temperature and increased antioxidant activity. Ara h1 conjugated with polyphenols may be a promising approach for reducing the allergenicity of Ara h1.
PB  - Elsevier
T2  - Food Chemistry
T1  - Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut
VL  - 331
SP  - 127355
DO  - 10.1016/j.foodchem.2020.127355
ER  - 

@article{
author = "He, Weiyi and Zhang, Tingting and Ćirković-Veličković, Tanja and Li, Shuiming and Lyu, Yansi and Wang, Linlin and Yi, Jiang and Liu, Zhigang and He, Zhendan and Wu, Xuli",
year = "2020",
abstract = "Ara h1 is a major allergen from peanut. We investigated the effect of covalent conjugation of Ara h1 and dietary polyphenols on allergenicity and functional properties of Ara h1. Enzyme-linked immunosorbent assay revealed that the covalent conjugation of dietary polyphenols significantly reduced the IgE binding capacity of Ara h1. Covalent binding of dietary polyphenols with Ara h1 reduced histamine release by 40% in basophils. The decreased IgE binding capacity of Ara h1 could be ascribed to changes in protein conformation. The IgE epitope of Ara h1 might be blocked by polyphenols at the binding site. Analysis of pepsin digestion of Ara h1–polyphenol conjugates indicated that the covalent binding increased pepsin digestibility and reduced IgE binding capacity. Furthermore, covalent conjugation of Ara h1 with polyphenols decreased denaturation temperature and increased antioxidant activity. Ara h1 conjugated with polyphenols may be a promising approach for reducing the allergenicity of Ara h1.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut",
volume = "331",
pages = "127355",
doi = "10.1016/j.foodchem.2020.127355"
}

He, W., Zhang, T., Ćirković-Veličković, T., Li, S., Lyu, Y., Wang, L., Yi, J., Liu, Z., He, Z.,& Wu, X.. (2020). Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut. in Food Chemistry
Elsevier., 331, 127355.
https://doi.org/10.1016/j.foodchem.2020.127355

He W, Zhang T, Ćirković-Veličković T, Li S, Lyu Y, Wang L, Yi J, Liu Z, He Z, Wu X. Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut. in Food Chemistry. 2020;331:127355.
doi:10.1016/j.foodchem.2020.127355 .

He, Weiyi, Zhang, Tingting, Ćirković-Veličković, Tanja, Li, Shuiming, Lyu, Yansi, Wang, Linlin, Yi, Jiang, Liu, Zhigang, He, Zhendan, Wu, Xuli, "Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut" in Food Chemistry, 331 (2020):127355,
https://doi.org/10.1016/j.foodchem.2020.127355 . .