Dextran sulfate acting as a chaperone-like component on inhibition of amorphous aggregation and enhancing thermal stability of ovotransferrin
•Dextran sulfate (DS) facilitates OVT to form soluble aggregates with higher charge, smaller size, more compact structure, and lower surface hydrophobicity.•The thermal tolerance of OVT against pasteurization was significantly improved by adding DS.•DS exhibited chaperone-like activities by preventi...
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Published in | Food chemistry Vol. 445; p. 138720 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
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England
Elsevier Ltd
01.07.2024
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Abstract | •Dextran sulfate (DS) facilitates OVT to form soluble aggregates with higher charge, smaller size, more compact structure, and lower surface hydrophobicity.•The thermal tolerance of OVT against pasteurization was significantly improved by adding DS.•DS exhibited chaperone-like activities by preventing protein aggregation and restoration of OVT structure.
The tendency of ovotransferrin (OVT) to unfold and aggregate under 60 °C severely restricted sterilization temperature during egg processing. Searching for efficient strategies to improve OVT thermal stability is essential for improving egg product quality and processing suitability. Here, we investigated the effect of sulfate polysaccharide (dextran sulfate, DS) on heat-induced aggregation of OVT. We found that DS can effectively suppress amorphous aggregation of OVT at pH 7.0 after heating. Strikingly, the addition of 5 µM DS fully suppressed insoluble aggregates formation of 0.5 mg/mL OVT. Structure analysis confirmed that DS preserves nearly the entire secondary and tertiary structure of OVT during heating. The steric hindrance effect arising from strong electrostatic interactions between OVT and DS, coupled with reduced OVT hydrophobicity, is the underlying mechanism in suppressing protein–protein interactions, thus enhancing thermal stability. These findings suggest DS could act as protein stabilizers and chaperones, enhancing the thermostability of heat-sensitive proteins. |
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AbstractList | The tendency of ovotransferrin (OVT) to unfold and aggregate under 60 °C severely restricted sterilization temperature during egg processing. Searching for efficient strategies to improve OVT thermal stability is essential for improving egg product quality and processing suitability. Here, we investigated the effect of sulfate polysaccharide (dextran sulfate, DS) on heat-induced aggregation of OVT. We found that DS can effectively suppress amorphous aggregation of OVT at pH 7.0 after heating. Strikingly, the addition of 5 µM DS fully suppressed insoluble aggregates formation of 0.5 mg/mL OVT. Structure analysis confirmed that DS preserves nearly the entire secondary and tertiary structure of OVT during heating. The steric hindrance effect arising from strong electrostatic interactions between OVT and DS, coupled with reduced OVT hydrophobicity, is the underlying mechanism in suppressing protein-protein interactions, thus enhancing thermal stability. These findings suggest DS could act as protein stabilizers and chaperones, enhancing the thermostability of heat-sensitive proteins. •Dextran sulfate (DS) facilitates OVT to form soluble aggregates with higher charge, smaller size, more compact structure, and lower surface hydrophobicity.•The thermal tolerance of OVT against pasteurization was significantly improved by adding DS.•DS exhibited chaperone-like activities by preventing protein aggregation and restoration of OVT structure. The tendency of ovotransferrin (OVT) to unfold and aggregate under 60 °C severely restricted sterilization temperature during egg processing. Searching for efficient strategies to improve OVT thermal stability is essential for improving egg product quality and processing suitability. Here, we investigated the effect of sulfate polysaccharide (dextran sulfate, DS) on heat-induced aggregation of OVT. We found that DS can effectively suppress amorphous aggregation of OVT at pH 7.0 after heating. Strikingly, the addition of 5 µM DS fully suppressed insoluble aggregates formation of 0.5 mg/mL OVT. Structure analysis confirmed that DS preserves nearly the entire secondary and tertiary structure of OVT during heating. The steric hindrance effect arising from strong electrostatic interactions between OVT and DS, coupled with reduced OVT hydrophobicity, is the underlying mechanism in suppressing protein–protein interactions, thus enhancing thermal stability. These findings suggest DS could act as protein stabilizers and chaperones, enhancing the thermostability of heat-sensitive proteins. The tendency of ovotransferrin (OVT) to unfold and aggregate under 60 °C severely restricted sterilization temperature during egg processing. Searching for efficient strategies to improve OVT thermal stability is essential for improving egg product quality and processing suitability. Here, we investigated the effect of sulfate polysaccharide (dextran sulfate, DS) on heat-induced aggregation of OVT. We found that DS can effectively suppress amorphous aggregation of OVT at pH 7.0 after heating. Strikingly, the addition of 5 µM DS fully suppressed insoluble aggregates formation of 0.5 mg/mL OVT. Structure analysis confirmed that DS preserves nearly the entire secondary and tertiary structure of OVT during heating. The steric hindrance effect arising from strong electrostatic interactions between OVT and DS, coupled with reduced OVT hydrophobicity, is the underlying mechanism in suppressing protein-protein interactions, thus enhancing thermal stability. These findings suggest DS could act as protein stabilizers and chaperones, enhancing the thermostability of heat-sensitive proteins. |
ArticleNumber | 138720 |
Author | Gong, Lingling Shang, Xiaomin Zhang, Ting Pan, Fengguang Wu, Xinling Yuan, Yixin Xu, Haojie Liu, Jingbo Lu, Jinming |
Author_xml | – sequence: 1 givenname: Fengguang surname: Pan fullname: Pan, Fengguang organization: Jilin Provincial Key Laboratory of Nutrition and Functional Food, Jilin University, Changchun 130062, PR China – sequence: 2 givenname: Xinling surname: Wu fullname: Wu, Xinling organization: Jilin Provincial Key Laboratory of Nutrition and Functional Food, Jilin University, Changchun 130062, PR China – sequence: 3 givenname: Lingling surname: Gong fullname: Gong, Lingling organization: Jilin Provincial Key Laboratory of Nutrition and Functional Food, Jilin University, Changchun 130062, PR China – sequence: 4 givenname: Haojie surname: Xu fullname: Xu, Haojie organization: Jilin Provincial Key Laboratory of Nutrition and Functional Food, Jilin University, Changchun 130062, PR China – sequence: 5 givenname: Yixin surname: Yuan fullname: Yuan, Yixin organization: Jilin Provincial Key Laboratory of Nutrition and Functional Food, Jilin University, Changchun 130062, PR China – sequence: 6 givenname: Jinming surname: Lu fullname: Lu, Jinming organization: College of Food Science and Engineering, Jilin University, Changchun 130062, PR China – sequence: 7 givenname: Ting surname: Zhang fullname: Zhang, Ting organization: Jilin Provincial Key Laboratory of Nutrition and Functional Food, Jilin University, Changchun 130062, PR China – sequence: 8 givenname: Jingbo surname: Liu fullname: Liu, Jingbo organization: Jilin Provincial Key Laboratory of Nutrition and Functional Food, Jilin University, Changchun 130062, PR China – sequence: 9 givenname: Xiaomin orcidid: 0000-0003-0538-2119 surname: Shang fullname: Shang, Xiaomin email: xmshang@jlu.edu.cn organization: Jilin Provincial Key Laboratory of Nutrition and Functional Food, Jilin University, Changchun 130062, PR China |
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Keywords | Chaperone-like activity Soluble aggregates Ovotransferrin Sulfated polysaccharide Thermal stability |
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Snippet | •Dextran sulfate (DS) facilitates OVT to form soluble aggregates with higher charge, smaller size, more compact structure, and lower surface... The tendency of ovotransferrin (OVT) to unfold and aggregate under 60 °C severely restricted sterilization temperature during egg processing. Searching for... The tendency of ovotransferrin (OVT) to unfold and aggregate under 60 °C severely restricted sterilization temperature during egg processing. Searching for... |
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SubjectTerms | Chaperone-like activity Conalbumin - chemistry Dextran Sulfate Hot Temperature Ovotransferrin Soluble aggregates Static Electricity Sulfated polysaccharide Temperature Thermal stability |
Title | Dextran sulfate acting as a chaperone-like component on inhibition of amorphous aggregation and enhancing thermal stability of ovotransferrin |
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