Enhancing the Antioxidant Activity of Fish Scale Collagen Hydrolysates Through Plastein Reaction
Abstract An important area of focus for developing antioxidant collagen hydrolysates (peptides) involves enhancing the antioxidant properties of collagen hydrolysates. In this study, fish scale collagen hydrolysate (FH) was used as the raw material for plastein reaction. Various enzymes, including p...
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| Autor*in: |
Xu, Chengzhi [verfasserIn] Cai, Chaonan [verfasserIn] Liu, Tianyi [verfasserIn] Kang, Jizhen [verfasserIn] Li, Sheng [verfasserIn] Zhang, Juntao [verfasserIn] Wei, Benmei [verfasserIn] Wang, Haibo [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2024 |
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| Schlagwörter: |
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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: Food and bioprocess technology - Springer US, 2008, 17(2024), 11 vom: 23. Feb., Seite 3693-3703 |
|---|---|
| Übergeordnetes Werk: |
volume:17 ; year:2024 ; number:11 ; day:23 ; month:02 ; pages:3693-3703 |
| Links: |
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| DOI / URN: |
10.1007/s11947-024-03329-9 |
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SPR057774927 |
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| 520 | |a Abstract An important area of focus for developing antioxidant collagen hydrolysates (peptides) involves enhancing the antioxidant properties of collagen hydrolysates. In this study, fish scale collagen hydrolysate (FH) was used as the raw material for plastein reaction. Various enzymes, including papain, alcalase, flavourzyme, and the combination of alcalase and flavourzyme, were employed for this purpose. The plastein reaction significantly improved the thermal stability, chemical antioxidant activity, and capacity to scavenge cellular reactive oxygen species of FH. Notably, the plastein reaction catalyzed by alcalase exhibited the most significant improvement, increasing the hydroxyl radical scavenging rate from 72.3 to 93.4% and restoring the viability of the oxidative stress-induced HepG2 cell model from 50.8 ± 1.7 to 74.9 ± 1.7%. During the plastein reaction, condensation and hydrolysis reactions occurred simultaneously, with condensation being the dominant process. These reactions, along with physical aggregation, facilitated the formation of larger yet more concentrated collagen peptide aggregates, leading to increased exposure of hydrophobic groups. This enhanced the uptake of collagen hydrolysates by the cells and contributed to the enhancement of their antioxidant properties. Thus, the plastein reaction is an effective method for enhancing the antioxidant properties of collagen hydrolysates, with its simplicity of operation and promising application potential. | ||
| 650 | 4 | |a Fish scale collagen hydrolysate |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Plastein reaction |7 (dpeaa)DE-He213 | |
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| 650 | 4 | |a Reactive oxygen species |7 (dpeaa)DE-He213 | |
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| 700 | 1 | |a Li, Sheng |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Juntao |e verfasserin |4 aut | |
| 700 | 1 | |a Wei, Benmei |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Haibo |e verfasserin |4 aut | |
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10.1007/s11947-024-03329-9 doi (DE-627)SPR057774927 (SPR)s11947-024-03329-9-e DE-627 ger DE-627 rakwb eng 660 VZ 58.34 bkl Xu, Chengzhi verfasserin aut Enhancing the Antioxidant Activity of Fish Scale Collagen Hydrolysates Through Plastein Reaction 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 An important area of focus for developing antioxidant collagen hydrolysates (peptides) involves enhancing the antioxidant properties of collagen hydrolysates. In this study, fish scale collagen hydrolysate (FH) was used as the raw material for plastein reaction. Various enzymes, including papain, alcalase, flavourzyme, and the combination of alcalase and flavourzyme, were employed for this purpose. The plastein reaction significantly improved the thermal stability, chemical antioxidant activity, and capacity to scavenge cellular reactive oxygen species of FH. Notably, the plastein reaction catalyzed by alcalase exhibited the most significant improvement, increasing the hydroxyl radical scavenging rate from 72.3 to 93.4% and restoring the viability of the oxidative stress-induced HepG2 cell model from 50.8 ± 1.7 to 74.9 ± 1.7%. During the plastein reaction, condensation and hydrolysis reactions occurred simultaneously, with condensation being the dominant process. These reactions, along with physical aggregation, facilitated the formation of larger yet more concentrated collagen peptide aggregates, leading to increased exposure of hydrophobic groups. This enhanced the uptake of collagen hydrolysates by the cells and contributed to the enhancement of their antioxidant properties. Thus, the plastein reaction is an effective method for enhancing the antioxidant properties of collagen hydrolysates, with its simplicity of operation and promising application potential. Fish scale collagen hydrolysate (dpeaa)DE-He213 Plastein reaction (dpeaa)DE-He213 Antioxidant properties (dpeaa)DE-He213 Reactive oxygen species (dpeaa)DE-He213 Cai, Chaonan verfasserin aut Liu, Tianyi verfasserin aut Kang, Jizhen verfasserin aut Li, Sheng verfasserin aut Zhang, Juntao verfasserin aut Wei, Benmei verfasserin aut Wang, Haibo verfasserin aut Enthalten in Food and bioprocess technology Springer US, 2008 17(2024), 11 vom: 23. Feb., Seite 3693-3703 (DE-627)566012294 (DE-600)2425455-1 1935-5149 nnns volume:17 year:2024 number:11 day:23 month:02 pages:3693-3703 https://dx.doi.org/10.1007/s11947-024-03329-9 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER SSG-OLC-PHA 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_120 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_2522 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_4313 GBV_ILN_4315 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_4700 58.34 VZ AR 17 2024 11 23 02 3693-3703 |
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10.1007/s11947-024-03329-9 doi (DE-627)SPR057774927 (SPR)s11947-024-03329-9-e DE-627 ger DE-627 rakwb eng 660 VZ 58.34 bkl Xu, Chengzhi verfasserin aut Enhancing the Antioxidant Activity of Fish Scale Collagen Hydrolysates Through Plastein Reaction 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 An important area of focus for developing antioxidant collagen hydrolysates (peptides) involves enhancing the antioxidant properties of collagen hydrolysates. In this study, fish scale collagen hydrolysate (FH) was used as the raw material for plastein reaction. Various enzymes, including papain, alcalase, flavourzyme, and the combination of alcalase and flavourzyme, were employed for this purpose. The plastein reaction significantly improved the thermal stability, chemical antioxidant activity, and capacity to scavenge cellular reactive oxygen species of FH. Notably, the plastein reaction catalyzed by alcalase exhibited the most significant improvement, increasing the hydroxyl radical scavenging rate from 72.3 to 93.4% and restoring the viability of the oxidative stress-induced HepG2 cell model from 50.8 ± 1.7 to 74.9 ± 1.7%. During the plastein reaction, condensation and hydrolysis reactions occurred simultaneously, with condensation being the dominant process. These reactions, along with physical aggregation, facilitated the formation of larger yet more concentrated collagen peptide aggregates, leading to increased exposure of hydrophobic groups. This enhanced the uptake of collagen hydrolysates by the cells and contributed to the enhancement of their antioxidant properties. Thus, the plastein reaction is an effective method for enhancing the antioxidant properties of collagen hydrolysates, with its simplicity of operation and promising application potential. Fish scale collagen hydrolysate (dpeaa)DE-He213 Plastein reaction (dpeaa)DE-He213 Antioxidant properties (dpeaa)DE-He213 Reactive oxygen species (dpeaa)DE-He213 Cai, Chaonan verfasserin aut Liu, Tianyi verfasserin aut Kang, Jizhen verfasserin aut Li, Sheng verfasserin aut Zhang, Juntao verfasserin aut Wei, Benmei verfasserin aut Wang, Haibo verfasserin aut Enthalten in Food and bioprocess technology Springer US, 2008 17(2024), 11 vom: 23. Feb., Seite 3693-3703 (DE-627)566012294 (DE-600)2425455-1 1935-5149 nnns volume:17 year:2024 number:11 day:23 month:02 pages:3693-3703 https://dx.doi.org/10.1007/s11947-024-03329-9 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER SSG-OLC-PHA 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_120 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_2522 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_4313 GBV_ILN_4315 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_4700 58.34 VZ AR 17 2024 11 23 02 3693-3703 |
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10.1007/s11947-024-03329-9 doi (DE-627)SPR057774927 (SPR)s11947-024-03329-9-e DE-627 ger DE-627 rakwb eng 660 VZ 58.34 bkl Xu, Chengzhi verfasserin aut Enhancing the Antioxidant Activity of Fish Scale Collagen Hydrolysates Through Plastein Reaction 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 An important area of focus for developing antioxidant collagen hydrolysates (peptides) involves enhancing the antioxidant properties of collagen hydrolysates. In this study, fish scale collagen hydrolysate (FH) was used as the raw material for plastein reaction. Various enzymes, including papain, alcalase, flavourzyme, and the combination of alcalase and flavourzyme, were employed for this purpose. The plastein reaction significantly improved the thermal stability, chemical antioxidant activity, and capacity to scavenge cellular reactive oxygen species of FH. Notably, the plastein reaction catalyzed by alcalase exhibited the most significant improvement, increasing the hydroxyl radical scavenging rate from 72.3 to 93.4% and restoring the viability of the oxidative stress-induced HepG2 cell model from 50.8 ± 1.7 to 74.9 ± 1.7%. During the plastein reaction, condensation and hydrolysis reactions occurred simultaneously, with condensation being the dominant process. These reactions, along with physical aggregation, facilitated the formation of larger yet more concentrated collagen peptide aggregates, leading to increased exposure of hydrophobic groups. This enhanced the uptake of collagen hydrolysates by the cells and contributed to the enhancement of their antioxidant properties. Thus, the plastein reaction is an effective method for enhancing the antioxidant properties of collagen hydrolysates, with its simplicity of operation and promising application potential. Fish scale collagen hydrolysate (dpeaa)DE-He213 Plastein reaction (dpeaa)DE-He213 Antioxidant properties (dpeaa)DE-He213 Reactive oxygen species (dpeaa)DE-He213 Cai, Chaonan verfasserin aut Liu, Tianyi verfasserin aut Kang, Jizhen verfasserin aut Li, Sheng verfasserin aut Zhang, Juntao verfasserin aut Wei, Benmei verfasserin aut Wang, Haibo verfasserin aut Enthalten in Food and bioprocess technology Springer US, 2008 17(2024), 11 vom: 23. Feb., Seite 3693-3703 (DE-627)566012294 (DE-600)2425455-1 1935-5149 nnns volume:17 year:2024 number:11 day:23 month:02 pages:3693-3703 https://dx.doi.org/10.1007/s11947-024-03329-9 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER SSG-OLC-PHA 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_120 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_2522 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_4313 GBV_ILN_4315 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_4700 58.34 VZ AR 17 2024 11 23 02 3693-3703 |
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10.1007/s11947-024-03329-9 doi (DE-627)SPR057774927 (SPR)s11947-024-03329-9-e DE-627 ger DE-627 rakwb eng 660 VZ 58.34 bkl Xu, Chengzhi verfasserin aut Enhancing the Antioxidant Activity of Fish Scale Collagen Hydrolysates Through Plastein Reaction 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 An important area of focus for developing antioxidant collagen hydrolysates (peptides) involves enhancing the antioxidant properties of collagen hydrolysates. In this study, fish scale collagen hydrolysate (FH) was used as the raw material for plastein reaction. Various enzymes, including papain, alcalase, flavourzyme, and the combination of alcalase and flavourzyme, were employed for this purpose. The plastein reaction significantly improved the thermal stability, chemical antioxidant activity, and capacity to scavenge cellular reactive oxygen species of FH. Notably, the plastein reaction catalyzed by alcalase exhibited the most significant improvement, increasing the hydroxyl radical scavenging rate from 72.3 to 93.4% and restoring the viability of the oxidative stress-induced HepG2 cell model from 50.8 ± 1.7 to 74.9 ± 1.7%. During the plastein reaction, condensation and hydrolysis reactions occurred simultaneously, with condensation being the dominant process. These reactions, along with physical aggregation, facilitated the formation of larger yet more concentrated collagen peptide aggregates, leading to increased exposure of hydrophobic groups. This enhanced the uptake of collagen hydrolysates by the cells and contributed to the enhancement of their antioxidant properties. Thus, the plastein reaction is an effective method for enhancing the antioxidant properties of collagen hydrolysates, with its simplicity of operation and promising application potential. Fish scale collagen hydrolysate (dpeaa)DE-He213 Plastein reaction (dpeaa)DE-He213 Antioxidant properties (dpeaa)DE-He213 Reactive oxygen species (dpeaa)DE-He213 Cai, Chaonan verfasserin aut Liu, Tianyi verfasserin aut Kang, Jizhen verfasserin aut Li, Sheng verfasserin aut Zhang, Juntao verfasserin aut Wei, Benmei verfasserin aut Wang, Haibo verfasserin aut Enthalten in Food and bioprocess technology Springer US, 2008 17(2024), 11 vom: 23. Feb., Seite 3693-3703 (DE-627)566012294 (DE-600)2425455-1 1935-5149 nnns volume:17 year:2024 number:11 day:23 month:02 pages:3693-3703 https://dx.doi.org/10.1007/s11947-024-03329-9 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER SSG-OLC-PHA 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_120 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_2522 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_4313 GBV_ILN_4315 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_4700 58.34 VZ AR 17 2024 11 23 02 3693-3703 |
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10.1007/s11947-024-03329-9 doi (DE-627)SPR057774927 (SPR)s11947-024-03329-9-e DE-627 ger DE-627 rakwb eng 660 VZ 58.34 bkl Xu, Chengzhi verfasserin aut Enhancing the Antioxidant Activity of Fish Scale Collagen Hydrolysates Through Plastein Reaction 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 An important area of focus for developing antioxidant collagen hydrolysates (peptides) involves enhancing the antioxidant properties of collagen hydrolysates. In this study, fish scale collagen hydrolysate (FH) was used as the raw material for plastein reaction. Various enzymes, including papain, alcalase, flavourzyme, and the combination of alcalase and flavourzyme, were employed for this purpose. The plastein reaction significantly improved the thermal stability, chemical antioxidant activity, and capacity to scavenge cellular reactive oxygen species of FH. Notably, the plastein reaction catalyzed by alcalase exhibited the most significant improvement, increasing the hydroxyl radical scavenging rate from 72.3 to 93.4% and restoring the viability of the oxidative stress-induced HepG2 cell model from 50.8 ± 1.7 to 74.9 ± 1.7%. During the plastein reaction, condensation and hydrolysis reactions occurred simultaneously, with condensation being the dominant process. These reactions, along with physical aggregation, facilitated the formation of larger yet more concentrated collagen peptide aggregates, leading to increased exposure of hydrophobic groups. This enhanced the uptake of collagen hydrolysates by the cells and contributed to the enhancement of their antioxidant properties. Thus, the plastein reaction is an effective method for enhancing the antioxidant properties of collagen hydrolysates, with its simplicity of operation and promising application potential. Fish scale collagen hydrolysate (dpeaa)DE-He213 Plastein reaction (dpeaa)DE-He213 Antioxidant properties (dpeaa)DE-He213 Reactive oxygen species (dpeaa)DE-He213 Cai, Chaonan verfasserin aut Liu, Tianyi verfasserin aut Kang, Jizhen verfasserin aut Li, Sheng verfasserin aut Zhang, Juntao verfasserin aut Wei, Benmei verfasserin aut Wang, Haibo verfasserin aut Enthalten in Food and bioprocess technology Springer US, 2008 17(2024), 11 vom: 23. Feb., Seite 3693-3703 (DE-627)566012294 (DE-600)2425455-1 1935-5149 nnns volume:17 year:2024 number:11 day:23 month:02 pages:3693-3703 https://dx.doi.org/10.1007/s11947-024-03329-9 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER SSG-OLC-PHA 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_120 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_2522 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_4313 GBV_ILN_4315 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_4700 58.34 VZ AR 17 2024 11 23 02 3693-3703 |
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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 An important area of focus for developing antioxidant collagen hydrolysates (peptides) involves enhancing the antioxidant properties of collagen hydrolysates. In this study, fish scale collagen hydrolysate (FH) was used as the raw material for plastein reaction. Various enzymes, including papain, alcalase, flavourzyme, and the combination of alcalase and flavourzyme, were employed for this purpose. The plastein reaction significantly improved the thermal stability, chemical antioxidant activity, and capacity to scavenge cellular reactive oxygen species of FH. Notably, the plastein reaction catalyzed by alcalase exhibited the most significant improvement, increasing the hydroxyl radical scavenging rate from 72.3 to 93.4% and restoring the viability of the oxidative stress-induced HepG2 cell model from 50.8 ± 1.7 to 74.9 ± 1.7%. During the plastein reaction, condensation and hydrolysis reactions occurred simultaneously, with condensation being the dominant process. These reactions, along with physical aggregation, facilitated the formation of larger yet more concentrated collagen peptide aggregates, leading to increased exposure of hydrophobic groups. This enhanced the uptake of collagen hydrolysates by the cells and contributed to the enhancement of their antioxidant properties. 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Xu, Chengzhi |
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enhancing the antioxidant activity of fish scale collagen hydrolysates through plastein reaction |
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Enhancing the Antioxidant Activity of Fish Scale Collagen Hydrolysates Through Plastein Reaction |
| abstract |
Abstract An important area of focus for developing antioxidant collagen hydrolysates (peptides) involves enhancing the antioxidant properties of collagen hydrolysates. In this study, fish scale collagen hydrolysate (FH) was used as the raw material for plastein reaction. Various enzymes, including papain, alcalase, flavourzyme, and the combination of alcalase and flavourzyme, were employed for this purpose. The plastein reaction significantly improved the thermal stability, chemical antioxidant activity, and capacity to scavenge cellular reactive oxygen species of FH. Notably, the plastein reaction catalyzed by alcalase exhibited the most significant improvement, increasing the hydroxyl radical scavenging rate from 72.3 to 93.4% and restoring the viability of the oxidative stress-induced HepG2 cell model from 50.8 ± 1.7 to 74.9 ± 1.7%. During the plastein reaction, condensation and hydrolysis reactions occurred simultaneously, with condensation being the dominant process. These reactions, along with physical aggregation, facilitated the formation of larger yet more concentrated collagen peptide aggregates, leading to increased exposure of hydrophobic groups. This enhanced the uptake of collagen hydrolysates by the cells and contributed to the enhancement of their antioxidant properties. Thus, the plastein reaction is an effective method for enhancing the antioxidant properties of collagen hydrolysates, with its simplicity of operation and promising application potential. © 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 An important area of focus for developing antioxidant collagen hydrolysates (peptides) involves enhancing the antioxidant properties of collagen hydrolysates. In this study, fish scale collagen hydrolysate (FH) was used as the raw material for plastein reaction. Various enzymes, including papain, alcalase, flavourzyme, and the combination of alcalase and flavourzyme, were employed for this purpose. The plastein reaction significantly improved the thermal stability, chemical antioxidant activity, and capacity to scavenge cellular reactive oxygen species of FH. Notably, the plastein reaction catalyzed by alcalase exhibited the most significant improvement, increasing the hydroxyl radical scavenging rate from 72.3 to 93.4% and restoring the viability of the oxidative stress-induced HepG2 cell model from 50.8 ± 1.7 to 74.9 ± 1.7%. During the plastein reaction, condensation and hydrolysis reactions occurred simultaneously, with condensation being the dominant process. These reactions, along with physical aggregation, facilitated the formation of larger yet more concentrated collagen peptide aggregates, leading to increased exposure of hydrophobic groups. This enhanced the uptake of collagen hydrolysates by the cells and contributed to the enhancement of their antioxidant properties. Thus, the plastein reaction is an effective method for enhancing the antioxidant properties of collagen hydrolysates, with its simplicity of operation and promising application potential. © 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 An important area of focus for developing antioxidant collagen hydrolysates (peptides) involves enhancing the antioxidant properties of collagen hydrolysates. In this study, fish scale collagen hydrolysate (FH) was used as the raw material for plastein reaction. Various enzymes, including papain, alcalase, flavourzyme, and the combination of alcalase and flavourzyme, were employed for this purpose. The plastein reaction significantly improved the thermal stability, chemical antioxidant activity, and capacity to scavenge cellular reactive oxygen species of FH. Notably, the plastein reaction catalyzed by alcalase exhibited the most significant improvement, increasing the hydroxyl radical scavenging rate from 72.3 to 93.4% and restoring the viability of the oxidative stress-induced HepG2 cell model from 50.8 ± 1.7 to 74.9 ± 1.7%. During the plastein reaction, condensation and hydrolysis reactions occurred simultaneously, with condensation being the dominant process. These reactions, along with physical aggregation, facilitated the formation of larger yet more concentrated collagen peptide aggregates, leading to increased exposure of hydrophobic groups. This enhanced the uptake of collagen hydrolysates by the cells and contributed to the enhancement of their antioxidant properties. Thus, the plastein reaction is an effective method for enhancing the antioxidant properties of collagen hydrolysates, with its simplicity of operation and promising application potential. © 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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| score |
7.4027834 |