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...

Full description

Saved in:
Bibliographic Details
Main Authors: Qian Cui, Yanqiu Ma, Xue Mao, Guozhi Zhao, Siyi Huang, Xingyu Wen, Zimeng Zhu, Xin Gao
Format: Article
Language:English
Published: Elsevier 2025-02-01
Series:Poultry Science
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S0032579125000537
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1832557608677933056
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