Protein-polyphenol conjugation through alkali treatment improves the structure and functionality of gluten
Abstract The conjugates of gluten and polyphenols (naringin, hesperetin or curcumin) were produced by alkaline method and the effects of conjugation on physicochemical properties of gluten were investigated in this study. The results show that the conjugates possess lower content of free amino and s...
Ausführliche Beschreibung
Autor*in: |
Liu, Jianying [verfasserIn] Ma, Yan [verfasserIn] Ukwatta, Ruchika Hansanie [verfasserIn] Xue, Feng [verfasserIn] Xiong, Xiaohui [verfasserIn] Li, Chen [verfasserIn] |
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E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2024 |
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Anmerkung: |
© The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. |
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Übergeordnetes Werk: |
Enthalten in: Journal of food measurement and characterization - Springer US, 2012, 18(2024), 10 vom: 09. Sept., Seite 8638-8650 |
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Übergeordnetes Werk: |
volume:18 ; year:2024 ; number:10 ; day:09 ; month:09 ; pages:8638-8650 |
Links: |
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DOI / URN: |
10.1007/s11694-024-02832-z |
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Katalog-ID: |
SPR058129928 |
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520 | |a Abstract The conjugates of gluten and polyphenols (naringin, hesperetin or curcumin) were produced by alkaline method and the effects of conjugation on physicochemical properties of gluten were investigated in this study. The results show that the conjugates possess lower content of free amino and sulfhydryl groups, and higher molecular mass, which indicate the covalent binding occurred. As compared with corresponding mixtures, the conjugates show lower intensity of the amide A, surface hydrophobicity, intermolecular β-sheets, interfacial and surface tension, as well as higher fluorescence intensity, antiparallel β-sheets and particle size (in the range of 130–150 μm). Furthermore, the conjugates also exhibit better emulsifying and foaming properties, higher storage modulus and lower degradation temperature than native gluten. However, the changes in physicochemical properties of conjugates depend on the type of polyphenols and curcumin-gluten conjugates possess the improved emulsifying, foaming and gelation properties among conjugates, due to their more flexible structure. | ||
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700 | 1 | |a Xue, Feng |e verfasserin |4 aut | |
700 | 1 | |a Xiong, Xiaohui |e verfasserin |4 aut | |
700 | 1 | |a Li, Chen |e verfasserin |0 (orcid)0000-0002-8135-8084 |4 aut | |
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10.1007/s11694-024-02832-z doi (DE-627)SPR058129928 (SPR)s11694-024-02832-z-e DE-627 ger DE-627 rakwb eng 630 640 VZ Liu, Jianying verfasserin aut Protein-polyphenol conjugation through alkali treatment improves the structure and functionality of gluten 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. Abstract The conjugates of gluten and polyphenols (naringin, hesperetin or curcumin) were produced by alkaline method and the effects of conjugation on physicochemical properties of gluten were investigated in this study. The results show that the conjugates possess lower content of free amino and sulfhydryl groups, and higher molecular mass, which indicate the covalent binding occurred. As compared with corresponding mixtures, the conjugates show lower intensity of the amide A, surface hydrophobicity, intermolecular β-sheets, interfacial and surface tension, as well as higher fluorescence intensity, antiparallel β-sheets and particle size (in the range of 130–150 μm). Furthermore, the conjugates also exhibit better emulsifying and foaming properties, higher storage modulus and lower degradation temperature than native gluten. However, the changes in physicochemical properties of conjugates depend on the type of polyphenols and curcumin-gluten conjugates possess the improved emulsifying, foaming and gelation properties among conjugates, due to their more flexible structure. Gluten (dpeaa)DE-He213 Naringin (dpeaa)DE-He213 Hesperetin (dpeaa)DE-He213 Curcumin (dpeaa)DE-He213 Conjugates (dpeaa)DE-He213 Ma, Yan verfasserin aut Ukwatta, Ruchika Hansanie verfasserin aut Xue, Feng verfasserin aut Xiong, Xiaohui verfasserin aut Li, Chen verfasserin (orcid)0000-0002-8135-8084 aut Enthalten in Journal of food measurement and characterization Springer US, 2012 18(2024), 10 vom: 09. Sept., Seite 8638-8650 Online-Ressource (DE-627)777234815 (DE-600)2754612-3 (DE-576)400527049 2193-4134 nnns volume:18 year:2024 number:10 day:09 month:09 pages:8638-8650 https://dx.doi.org/10.1007/s11694-024-02832-z X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2548 GBV_ILN_2574 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4315 GBV_ILN_4317 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 18 2024 10 09 09 8638-8650 |
spelling |
10.1007/s11694-024-02832-z doi (DE-627)SPR058129928 (SPR)s11694-024-02832-z-e DE-627 ger DE-627 rakwb eng 630 640 VZ Liu, Jianying verfasserin aut Protein-polyphenol conjugation through alkali treatment improves the structure and functionality of gluten 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. Abstract The conjugates of gluten and polyphenols (naringin, hesperetin or curcumin) were produced by alkaline method and the effects of conjugation on physicochemical properties of gluten were investigated in this study. The results show that the conjugates possess lower content of free amino and sulfhydryl groups, and higher molecular mass, which indicate the covalent binding occurred. As compared with corresponding mixtures, the conjugates show lower intensity of the amide A, surface hydrophobicity, intermolecular β-sheets, interfacial and surface tension, as well as higher fluorescence intensity, antiparallel β-sheets and particle size (in the range of 130–150 μm). Furthermore, the conjugates also exhibit better emulsifying and foaming properties, higher storage modulus and lower degradation temperature than native gluten. However, the changes in physicochemical properties of conjugates depend on the type of polyphenols and curcumin-gluten conjugates possess the improved emulsifying, foaming and gelation properties among conjugates, due to their more flexible structure. Gluten (dpeaa)DE-He213 Naringin (dpeaa)DE-He213 Hesperetin (dpeaa)DE-He213 Curcumin (dpeaa)DE-He213 Conjugates (dpeaa)DE-He213 Ma, Yan verfasserin aut Ukwatta, Ruchika Hansanie verfasserin aut Xue, Feng verfasserin aut Xiong, Xiaohui verfasserin aut Li, Chen verfasserin (orcid)0000-0002-8135-8084 aut Enthalten in Journal of food measurement and characterization Springer US, 2012 18(2024), 10 vom: 09. Sept., Seite 8638-8650 Online-Ressource (DE-627)777234815 (DE-600)2754612-3 (DE-576)400527049 2193-4134 nnns volume:18 year:2024 number:10 day:09 month:09 pages:8638-8650 https://dx.doi.org/10.1007/s11694-024-02832-z X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2548 GBV_ILN_2574 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4315 GBV_ILN_4317 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 18 2024 10 09 09 8638-8650 |
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10.1007/s11694-024-02832-z doi (DE-627)SPR058129928 (SPR)s11694-024-02832-z-e DE-627 ger DE-627 rakwb eng 630 640 VZ Liu, Jianying verfasserin aut Protein-polyphenol conjugation through alkali treatment improves the structure and functionality of gluten 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. Abstract The conjugates of gluten and polyphenols (naringin, hesperetin or curcumin) were produced by alkaline method and the effects of conjugation on physicochemical properties of gluten were investigated in this study. The results show that the conjugates possess lower content of free amino and sulfhydryl groups, and higher molecular mass, which indicate the covalent binding occurred. As compared with corresponding mixtures, the conjugates show lower intensity of the amide A, surface hydrophobicity, intermolecular β-sheets, interfacial and surface tension, as well as higher fluorescence intensity, antiparallel β-sheets and particle size (in the range of 130–150 μm). Furthermore, the conjugates also exhibit better emulsifying and foaming properties, higher storage modulus and lower degradation temperature than native gluten. However, the changes in physicochemical properties of conjugates depend on the type of polyphenols and curcumin-gluten conjugates possess the improved emulsifying, foaming and gelation properties among conjugates, due to their more flexible structure. Gluten (dpeaa)DE-He213 Naringin (dpeaa)DE-He213 Hesperetin (dpeaa)DE-He213 Curcumin (dpeaa)DE-He213 Conjugates (dpeaa)DE-He213 Ma, Yan verfasserin aut Ukwatta, Ruchika Hansanie verfasserin aut Xue, Feng verfasserin aut Xiong, Xiaohui verfasserin aut Li, Chen verfasserin (orcid)0000-0002-8135-8084 aut Enthalten in Journal of food measurement and characterization Springer US, 2012 18(2024), 10 vom: 09. Sept., Seite 8638-8650 Online-Ressource (DE-627)777234815 (DE-600)2754612-3 (DE-576)400527049 2193-4134 nnns volume:18 year:2024 number:10 day:09 month:09 pages:8638-8650 https://dx.doi.org/10.1007/s11694-024-02832-z X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2548 GBV_ILN_2574 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4315 GBV_ILN_4317 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 18 2024 10 09 09 8638-8650 |
allfieldsGer |
10.1007/s11694-024-02832-z doi (DE-627)SPR058129928 (SPR)s11694-024-02832-z-e DE-627 ger DE-627 rakwb eng 630 640 VZ Liu, Jianying verfasserin aut Protein-polyphenol conjugation through alkali treatment improves the structure and functionality of gluten 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. Abstract The conjugates of gluten and polyphenols (naringin, hesperetin or curcumin) were produced by alkaline method and the effects of conjugation on physicochemical properties of gluten were investigated in this study. The results show that the conjugates possess lower content of free amino and sulfhydryl groups, and higher molecular mass, which indicate the covalent binding occurred. As compared with corresponding mixtures, the conjugates show lower intensity of the amide A, surface hydrophobicity, intermolecular β-sheets, interfacial and surface tension, as well as higher fluorescence intensity, antiparallel β-sheets and particle size (in the range of 130–150 μm). Furthermore, the conjugates also exhibit better emulsifying and foaming properties, higher storage modulus and lower degradation temperature than native gluten. However, the changes in physicochemical properties of conjugates depend on the type of polyphenols and curcumin-gluten conjugates possess the improved emulsifying, foaming and gelation properties among conjugates, due to their more flexible structure. Gluten (dpeaa)DE-He213 Naringin (dpeaa)DE-He213 Hesperetin (dpeaa)DE-He213 Curcumin (dpeaa)DE-He213 Conjugates (dpeaa)DE-He213 Ma, Yan verfasserin aut Ukwatta, Ruchika Hansanie verfasserin aut Xue, Feng verfasserin aut Xiong, Xiaohui verfasserin aut Li, Chen verfasserin (orcid)0000-0002-8135-8084 aut Enthalten in Journal of food measurement and characterization Springer US, 2012 18(2024), 10 vom: 09. Sept., Seite 8638-8650 Online-Ressource (DE-627)777234815 (DE-600)2754612-3 (DE-576)400527049 2193-4134 nnns volume:18 year:2024 number:10 day:09 month:09 pages:8638-8650 https://dx.doi.org/10.1007/s11694-024-02832-z X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2548 GBV_ILN_2574 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4315 GBV_ILN_4317 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 18 2024 10 09 09 8638-8650 |
allfieldsSound |
10.1007/s11694-024-02832-z doi (DE-627)SPR058129928 (SPR)s11694-024-02832-z-e DE-627 ger DE-627 rakwb eng 630 640 VZ Liu, Jianying verfasserin aut Protein-polyphenol conjugation through alkali treatment improves the structure and functionality of gluten 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. Abstract The conjugates of gluten and polyphenols (naringin, hesperetin or curcumin) were produced by alkaline method and the effects of conjugation on physicochemical properties of gluten were investigated in this study. The results show that the conjugates possess lower content of free amino and sulfhydryl groups, and higher molecular mass, which indicate the covalent binding occurred. As compared with corresponding mixtures, the conjugates show lower intensity of the amide A, surface hydrophobicity, intermolecular β-sheets, interfacial and surface tension, as well as higher fluorescence intensity, antiparallel β-sheets and particle size (in the range of 130–150 μm). Furthermore, the conjugates also exhibit better emulsifying and foaming properties, higher storage modulus and lower degradation temperature than native gluten. However, the changes in physicochemical properties of conjugates depend on the type of polyphenols and curcumin-gluten conjugates possess the improved emulsifying, foaming and gelation properties among conjugates, due to their more flexible structure. Gluten (dpeaa)DE-He213 Naringin (dpeaa)DE-He213 Hesperetin (dpeaa)DE-He213 Curcumin (dpeaa)DE-He213 Conjugates (dpeaa)DE-He213 Ma, Yan verfasserin aut Ukwatta, Ruchika Hansanie verfasserin aut Xue, Feng verfasserin aut Xiong, Xiaohui verfasserin aut Li, Chen verfasserin (orcid)0000-0002-8135-8084 aut Enthalten in Journal of food measurement and characterization Springer US, 2012 18(2024), 10 vom: 09. Sept., Seite 8638-8650 Online-Ressource (DE-627)777234815 (DE-600)2754612-3 (DE-576)400527049 2193-4134 nnns volume:18 year:2024 number:10 day:09 month:09 pages:8638-8650 https://dx.doi.org/10.1007/s11694-024-02832-z X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2548 GBV_ILN_2574 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4315 GBV_ILN_4317 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 18 2024 10 09 09 8638-8650 |
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Enthalten in Journal of food measurement and characterization 18(2024), 10 vom: 09. Sept., Seite 8638-8650 volume:18 year:2024 number:10 day:09 month:09 pages:8638-8650 |
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Gluten Naringin Hesperetin Curcumin Conjugates |
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Liu, Jianying @@aut@@ Ma, Yan @@aut@@ Ukwatta, Ruchika Hansanie @@aut@@ Xue, Feng @@aut@@ Xiong, Xiaohui @@aut@@ Li, Chen @@aut@@ |
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Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract The conjugates of gluten and polyphenols (naringin, hesperetin or curcumin) were produced by alkaline method and the effects of conjugation on physicochemical properties of gluten were investigated in this study. The results show that the conjugates possess lower content of free amino and sulfhydryl groups, and higher molecular mass, which indicate the covalent binding occurred. As compared with corresponding mixtures, the conjugates show lower intensity of the amide A, surface hydrophobicity, intermolecular β-sheets, interfacial and surface tension, as well as higher fluorescence intensity, antiparallel β-sheets and particle size (in the range of 130–150 μm). Furthermore, the conjugates also exhibit better emulsifying and foaming properties, higher storage modulus and lower degradation temperature than native gluten. 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Liu, Jianying |
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Liu, Jianying ddc 630 misc Gluten misc Naringin misc Hesperetin misc Curcumin misc Conjugates Protein-polyphenol conjugation through alkali treatment improves the structure and functionality of gluten |
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630 640 VZ Protein-polyphenol conjugation through alkali treatment improves the structure and functionality of gluten Gluten (dpeaa)DE-He213 Naringin (dpeaa)DE-He213 Hesperetin (dpeaa)DE-He213 Curcumin (dpeaa)DE-He213 Conjugates (dpeaa)DE-He213 |
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Protein-polyphenol conjugation through alkali treatment improves the structure and functionality of gluten |
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Protein-polyphenol conjugation through alkali treatment improves the structure and functionality of gluten |
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protein-polyphenol conjugation through alkali treatment improves the structure and functionality of gluten |
title_auth |
Protein-polyphenol conjugation through alkali treatment improves the structure and functionality of gluten |
abstract |
Abstract The conjugates of gluten and polyphenols (naringin, hesperetin or curcumin) were produced by alkaline method and the effects of conjugation on physicochemical properties of gluten were investigated in this study. The results show that the conjugates possess lower content of free amino and sulfhydryl groups, and higher molecular mass, which indicate the covalent binding occurred. As compared with corresponding mixtures, the conjugates show lower intensity of the amide A, surface hydrophobicity, intermolecular β-sheets, interfacial and surface tension, as well as higher fluorescence intensity, antiparallel β-sheets and particle size (in the range of 130–150 μm). Furthermore, the conjugates also exhibit better emulsifying and foaming properties, higher storage modulus and lower degradation temperature than native gluten. However, the changes in physicochemical properties of conjugates depend on the type of polyphenols and curcumin-gluten conjugates possess the improved emulsifying, foaming and gelation properties among conjugates, due to their more flexible structure. © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. |
abstractGer |
Abstract The conjugates of gluten and polyphenols (naringin, hesperetin or curcumin) were produced by alkaline method and the effects of conjugation on physicochemical properties of gluten were investigated in this study. The results show that the conjugates possess lower content of free amino and sulfhydryl groups, and higher molecular mass, which indicate the covalent binding occurred. As compared with corresponding mixtures, the conjugates show lower intensity of the amide A, surface hydrophobicity, intermolecular β-sheets, interfacial and surface tension, as well as higher fluorescence intensity, antiparallel β-sheets and particle size (in the range of 130–150 μm). Furthermore, the conjugates also exhibit better emulsifying and foaming properties, higher storage modulus and lower degradation temperature than native gluten. However, the changes in physicochemical properties of conjugates depend on the type of polyphenols and curcumin-gluten conjugates possess the improved emulsifying, foaming and gelation properties among conjugates, due to their more flexible structure. © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. |
abstract_unstemmed |
Abstract The conjugates of gluten and polyphenols (naringin, hesperetin or curcumin) were produced by alkaline method and the effects of conjugation on physicochemical properties of gluten were investigated in this study. The results show that the conjugates possess lower content of free amino and sulfhydryl groups, and higher molecular mass, which indicate the covalent binding occurred. As compared with corresponding mixtures, the conjugates show lower intensity of the amide A, surface hydrophobicity, intermolecular β-sheets, interfacial and surface tension, as well as higher fluorescence intensity, antiparallel β-sheets and particle size (in the range of 130–150 μm). Furthermore, the conjugates also exhibit better emulsifying and foaming properties, higher storage modulus and lower degradation temperature than native gluten. However, the changes in physicochemical properties of conjugates depend on the type of polyphenols and curcumin-gluten conjugates possess the improved emulsifying, foaming and gelation properties among conjugates, due to their more flexible structure. © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. |
collection_details |
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container_issue |
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title_short |
Protein-polyphenol conjugation through alkali treatment improves the structure and functionality of gluten |
url |
https://dx.doi.org/10.1007/s11694-024-02832-z |
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Ma, Yan Ukwatta, Ruchika Hansanie Xue, Feng Xiong, Xiaohui Li, Chen |
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score |
7.4002647 |