Effect of rutin on the structural and functional properties of ovalbumin
Phenolic substances affect protein functionality. This study aimed to examine how rutin influences the gel properties, antioxidant activity, and structure of ovalbumin (OVA). Increasing rutin concentration enhanced the gel hardness of OVA but reduced soluble protein content with no significant effec...
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Elsevier
2025-02-01
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Series: | Poultry Science |
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Online Access: | http://www.sciencedirect.com/science/article/pii/S0032579125000537 |
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author | Qian Cui Yanqiu Ma Xue Mao Guozhi Zhao Siyi Huang Xingyu Wen Zimeng Zhu Xin Gao |
author_facet | Qian Cui Yanqiu Ma Xue Mao Guozhi Zhao Siyi Huang Xingyu Wen Zimeng Zhu Xin Gao |
author_sort | Qian Cui |
collection | DOAJ |
description | Phenolic substances affect protein functionality. This study aimed to examine how rutin influences the gel properties, antioxidant activity, and structure of ovalbumin (OVA). Increasing rutin concentration enhanced the gel hardness of OVA but reduced soluble protein content with no significant effect on water retention. At 0.25 % rutin concentration, the gel hardness of OVA increased from 109.33 g to 292.60 g, while soluble protein content decreased from 1.08 mg/mL to 0.97 mg/mL. Rutin modification significantly increased the storage and loss moduli of OVA gel, making its structure more compact. At 0.25 % rutin, antioxidant analysis showed increases in the DPPH radical scavenging rate (127 %), ABTS radical scavenging rate (112 %), hydroxyl radical scavenging rate (4167 %), and reducing power (101 %) of OVA. Fluorescence spectroscopy, surface hydrophobicity, free sulfhydryl content, and circular dichroism spectra revealed that higher rutin concentrations reduced fluorescence intensity and surface hydrophobicity while increasing the free sulfhydryl content of OVA. The α-helix content of OVA decreased, while β-sheet content increased. In addition, it was confirmed that OVA and rutin were bound by hydrophobic interaction. The quenching mechanism was static quenching. Rutin alters the structure and functional properties of OVA, providing a theoretical foundation for developing antioxidant and high-gel OVA variants. |
format | Article |
id | doaj-art-eaa4de64a102483a977dc869b35a8c56 |
institution | Kabale University |
issn | 0032-5791 |
language | English |
publishDate | 2025-02-01 |
publisher | Elsevier |
record_format | Article |
series | Poultry Science |
spelling | doaj-art-eaa4de64a102483a977dc869b35a8c562025-02-03T04:16:26ZengElsevierPoultry Science0032-57912025-02-011042104816Effect of rutin on the structural and functional properties of ovalbuminQian Cui0Yanqiu Ma1Xue Mao2Guozhi Zhao3Siyi Huang4Xingyu Wen5Zimeng Zhu6Xin Gao7College of Food Science, Northeast Agricultural University, Harbin 150030, PR ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, PR ChinaHeilongjiang Academy of Sciences Institute of Microbiology, Harbin 150010, PR ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, PR ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, PR ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, PR ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, PR ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, PR China; Corresponding author at: College of Food Science, Northeast Agricultural University, Harbin, 150030, PR ChinaPhenolic substances affect protein functionality. This study aimed to examine how rutin influences the gel properties, antioxidant activity, and structure of ovalbumin (OVA). Increasing rutin concentration enhanced the gel hardness of OVA but reduced soluble protein content with no significant effect on water retention. At 0.25 % rutin concentration, the gel hardness of OVA increased from 109.33 g to 292.60 g, while soluble protein content decreased from 1.08 mg/mL to 0.97 mg/mL. Rutin modification significantly increased the storage and loss moduli of OVA gel, making its structure more compact. At 0.25 % rutin, antioxidant analysis showed increases in the DPPH radical scavenging rate (127 %), ABTS radical scavenging rate (112 %), hydroxyl radical scavenging rate (4167 %), and reducing power (101 %) of OVA. Fluorescence spectroscopy, surface hydrophobicity, free sulfhydryl content, and circular dichroism spectra revealed that higher rutin concentrations reduced fluorescence intensity and surface hydrophobicity while increasing the free sulfhydryl content of OVA. The α-helix content of OVA decreased, while β-sheet content increased. In addition, it was confirmed that OVA and rutin were bound by hydrophobic interaction. The quenching mechanism was static quenching. Rutin alters the structure and functional properties of OVA, providing a theoretical foundation for developing antioxidant and high-gel OVA variants.http://www.sciencedirect.com/science/article/pii/S0032579125000537OvalbuminRutinGel propertyAntioxidant activity |
spellingShingle | Qian Cui Yanqiu Ma Xue Mao Guozhi Zhao Siyi Huang Xingyu Wen Zimeng Zhu Xin Gao Effect of rutin on the structural and functional properties of ovalbumin Poultry Science Ovalbumin Rutin Gel property Antioxidant activity |
title | Effect of rutin on the structural and functional properties of ovalbumin |
title_full | Effect of rutin on the structural and functional properties of ovalbumin |
title_fullStr | Effect of rutin on the structural and functional properties of ovalbumin |
title_full_unstemmed | Effect of rutin on the structural and functional properties of ovalbumin |
title_short | Effect of rutin on the structural and functional properties of ovalbumin |
title_sort | effect of rutin on the structural and functional properties of ovalbumin |
topic | Ovalbumin Rutin Gel property Antioxidant activity |
url | http://www.sciencedirect.com/science/article/pii/S0032579125000537 |
work_keys_str_mv | AT qiancui effectofrutinonthestructuralandfunctionalpropertiesofovalbumin AT yanqiuma effectofrutinonthestructuralandfunctionalpropertiesofovalbumin AT xuemao effectofrutinonthestructuralandfunctionalpropertiesofovalbumin AT guozhizhao effectofrutinonthestructuralandfunctionalpropertiesofovalbumin AT siyihuang effectofrutinonthestructuralandfunctionalpropertiesofovalbumin AT xingyuwen effectofrutinonthestructuralandfunctionalpropertiesofovalbumin AT zimengzhu effectofrutinonthestructuralandfunctionalpropertiesofovalbumin AT xingao effectofrutinonthestructuralandfunctionalpropertiesofovalbumin |