The Thermodynamic and Gelation Properties of Ovalbumin and Lysozyme
Ovalbumin (OVA) and lysozyme (LYZ) are the predominant globular proteins in egg white and play a crucial role in influencing thermal stability and colloidal behavior. In this study, the thermal and conformational stability of OVA and LYZ under various physicochemical conditions including pH (5–9), p...
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2025-06-01
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| author | Lifeng Wang Rongcheng Li Siyi Lv Yulin Liu Shuaifu Fang Jingnan Zang Mingmin Qing Yujie Chi |
| author_facet | Lifeng Wang Rongcheng Li Siyi Lv Yulin Liu Shuaifu Fang Jingnan Zang Mingmin Qing Yujie Chi |
| author_sort | Lifeng Wang |
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| description | Ovalbumin (OVA) and lysozyme (LYZ) are the predominant globular proteins in egg white and play a crucial role in influencing thermal stability and colloidal behavior. In this study, the thermal and conformational stability of OVA and LYZ under various physicochemical conditions including pH (5–9), protein concentrations (5, 10, and 20%), heating rates (2.5, 5, and 10 °C/min), sugars (sucrose and glucose), and salts (NaCl, KCl, and CaCl<sub>2</sub>) was systematically investigated using differential scanning calorimetry (DSC), aiming to elucidate their behavior within colloidal and gel-forming systems. The denaturation temperatures (T<sub>d</sub>) of OVA and LYZ in water (5% <i>w</i>/<i>v</i>, 5 °C/min) were 80.22 °C and 77.46 °C, respectively. The T<sub>d</sub> of LYZ and OVA decreased with protein concentration, heating rate, and CaCl<sub>2</sub>. OVA thermal stability was improved with increasing pH, but the stability of LYZ was decreased. Sugars enhanced the thermal stability of OVA and LYZ. In contrast, NaCl and KCl increased OVA stability but reduced LYZ stability. LYZ exhibited nearly 100% reversibility during the second heating cycle in water. Sugars maintained reversibility at approximately 90% for LYZ. However, the presence of salts diminished the reversibility. In contrast, OVA was completely denatured in water and sugar and salt solutions. |
| format | Article |
| id | doaj-art-831f4d0c86d74b928ed687031fee772c |
| institution | Kabale University |
| issn | 2310-2861 |
| language | English |
| publishDate | 2025-06-01 |
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| spelling | doaj-art-831f4d0c86d74b928ed687031fee772c2025-08-20T03:24:36ZengMDPI AGGels2310-28612025-06-0111647010.3390/gels11060470The Thermodynamic and Gelation Properties of Ovalbumin and LysozymeLifeng Wang0Rongcheng Li1Siyi Lv2Yulin Liu3Shuaifu Fang4Jingnan Zang5Mingmin Qing6Yujie Chi7College of Food Science, Northeast Agricultural University, Harbin 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, ChinaCollege of Food Science, Northeast Agricultural University, Harbin 150030, ChinaOvalbumin (OVA) and lysozyme (LYZ) are the predominant globular proteins in egg white and play a crucial role in influencing thermal stability and colloidal behavior. In this study, the thermal and conformational stability of OVA and LYZ under various physicochemical conditions including pH (5–9), protein concentrations (5, 10, and 20%), heating rates (2.5, 5, and 10 °C/min), sugars (sucrose and glucose), and salts (NaCl, KCl, and CaCl<sub>2</sub>) was systematically investigated using differential scanning calorimetry (DSC), aiming to elucidate their behavior within colloidal and gel-forming systems. The denaturation temperatures (T<sub>d</sub>) of OVA and LYZ in water (5% <i>w</i>/<i>v</i>, 5 °C/min) were 80.22 °C and 77.46 °C, respectively. The T<sub>d</sub> of LYZ and OVA decreased with protein concentration, heating rate, and CaCl<sub>2</sub>. OVA thermal stability was improved with increasing pH, but the stability of LYZ was decreased. Sugars enhanced the thermal stability of OVA and LYZ. In contrast, NaCl and KCl increased OVA stability but reduced LYZ stability. LYZ exhibited nearly 100% reversibility during the second heating cycle in water. Sugars maintained reversibility at approximately 90% for LYZ. However, the presence of salts diminished the reversibility. In contrast, OVA was completely denatured in water and sugar and salt solutions.https://www.mdpi.com/2310-2861/11/6/470DSCthermal denaturationovalbuminlysozymereversibility |
| spellingShingle | Lifeng Wang Rongcheng Li Siyi Lv Yulin Liu Shuaifu Fang Jingnan Zang Mingmin Qing Yujie Chi The Thermodynamic and Gelation Properties of Ovalbumin and Lysozyme Gels DSC thermal denaturation ovalbumin lysozyme reversibility |
| title | The Thermodynamic and Gelation Properties of Ovalbumin and Lysozyme |
| title_full | The Thermodynamic and Gelation Properties of Ovalbumin and Lysozyme |
| title_fullStr | The Thermodynamic and Gelation Properties of Ovalbumin and Lysozyme |
| title_full_unstemmed | The Thermodynamic and Gelation Properties of Ovalbumin and Lysozyme |
| title_short | The Thermodynamic and Gelation Properties of Ovalbumin and Lysozyme |
| title_sort | thermodynamic and gelation properties of ovalbumin and lysozyme |
| topic | DSC thermal denaturation ovalbumin lysozyme reversibility |
| url | https://www.mdpi.com/2310-2861/11/6/470 |
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