3D Printability of Lysine-Modified Myofibrillar Protein Emulsions
This study explores the potential of lysine (Lys) and tilapia myofibrillar protein (MP) composite particles in the formulation of highly inwardly directed emulsions (HIPEs). Infrared spectroscopy, potentiometric analysis, and molecular docking studies revealed that the interaction between Lys and MP...
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MDPI AG
2025-06-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/14/12/2138 |
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| author | Lin Liao Zilan Feng Yoon-Yen Yow Yajie Song Yuxiao Liu Lixiang Qin Xiaofei Wu Zhisheng Pei Changfeng Xue |
| author_facet | Lin Liao Zilan Feng Yoon-Yen Yow Yajie Song Yuxiao Liu Lixiang Qin Xiaofei Wu Zhisheng Pei Changfeng Xue |
| author_sort | Lin Liao |
| collection | DOAJ |
| description | This study explores the potential of lysine (Lys) and tilapia myofibrillar protein (MP) composite particles in the formulation of highly inwardly directed emulsions (HIPEs). Infrared spectroscopy, potentiometric analysis, and molecular docking studies revealed that the interaction between Lys and MP is primarily governed by hydrogen bonding and electrostatic forces. The incorporation of Lys significantly influenced the particle size, secondary and tertiary structures, solubility, and turbidity of MP. Lys-MP-stabilized HIPEs can form highly stable denser self-supporting gel network structures. Rheological analysis of HIPEs stabilized by MP showed a low energy storage modulus (G’ 110.66 Pa) and water–oil separation, therefore preventing 3D printing. However, HIPEs stabilized by Lys (especially 1.5 wt%) significantly improved the energy storage modulus (G’ 1002.10 Pa), increased viscoelasticity and thixotropic recovery, and reduced droplet size (10.84 μm), facilitating the use of HIPE inks for 3D printing. Furthermore, HIPEs stabilized with 1.5 wt% Lys-MP demonstrated superior print accuracy (91.36%), resolution, and clarity in 3D printing applications. Overall, these findings offer a promising strategy for developing Lys-MP composite particle-stabilized HIPEs tailored for advanced 3D printing technologies. |
| format | Article |
| id | doaj-art-ba590c53544e4ab3bb0d1a9636c216b6 |
| institution | Kabale University |
| issn | 2304-8158 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj-art-ba590c53544e4ab3bb0d1a9636c216b62025-08-20T03:24:40ZengMDPI AGFoods2304-81582025-06-011412213810.3390/foods141221383D Printability of Lysine-Modified Myofibrillar Protein EmulsionsLin Liao0Zilan Feng1Yoon-Yen Yow2Yajie Song3Yuxiao Liu4Lixiang Qin5Xiaofei Wu6Zhisheng Pei7Changfeng Xue8School of Food Science and Engineering, Hainan Tropical Ocean University, Sanya 572022, ChinaSchool of Food Science and Engineering, Hainan University, Haikou 570228, ChinaDepartment of Biomedical Sciences, Sir Jeffrey Cheah Sunway Medical School, Faculty of Medical and Life Sciences, Sunway University, Sunway City 47500, MalaysiaSchool of Food Science and Engineering, Hainan Tropical Ocean University, Sanya 572022, ChinaSchool of Food Science and Engineering, Hainan Tropical Ocean University, Sanya 572022, ChinaSchool of Food Science and Engineering, Hainan Tropical Ocean University, Sanya 572022, ChinaSchool of Food Science and Engineering, Hainan Tropical Ocean University, Sanya 572022, ChinaSchool of Food Science and Engineering, Hainan Tropical Ocean University, Sanya 572022, ChinaSchool of Food Science and Engineering, Hainan Tropical Ocean University, Sanya 572022, ChinaThis study explores the potential of lysine (Lys) and tilapia myofibrillar protein (MP) composite particles in the formulation of highly inwardly directed emulsions (HIPEs). Infrared spectroscopy, potentiometric analysis, and molecular docking studies revealed that the interaction between Lys and MP is primarily governed by hydrogen bonding and electrostatic forces. The incorporation of Lys significantly influenced the particle size, secondary and tertiary structures, solubility, and turbidity of MP. Lys-MP-stabilized HIPEs can form highly stable denser self-supporting gel network structures. Rheological analysis of HIPEs stabilized by MP showed a low energy storage modulus (G’ 110.66 Pa) and water–oil separation, therefore preventing 3D printing. However, HIPEs stabilized by Lys (especially 1.5 wt%) significantly improved the energy storage modulus (G’ 1002.10 Pa), increased viscoelasticity and thixotropic recovery, and reduced droplet size (10.84 μm), facilitating the use of HIPE inks for 3D printing. Furthermore, HIPEs stabilized with 1.5 wt% Lys-MP demonstrated superior print accuracy (91.36%), resolution, and clarity in 3D printing applications. Overall, these findings offer a promising strategy for developing Lys-MP composite particle-stabilized HIPEs tailored for advanced 3D printing technologies.https://www.mdpi.com/2304-8158/14/12/2138lysinemyofibrillar proteinHIPEs3D printability |
| spellingShingle | Lin Liao Zilan Feng Yoon-Yen Yow Yajie Song Yuxiao Liu Lixiang Qin Xiaofei Wu Zhisheng Pei Changfeng Xue 3D Printability of Lysine-Modified Myofibrillar Protein Emulsions Foods lysine myofibrillar protein HIPEs 3D printability |
| title | 3D Printability of Lysine-Modified Myofibrillar Protein Emulsions |
| title_full | 3D Printability of Lysine-Modified Myofibrillar Protein Emulsions |
| title_fullStr | 3D Printability of Lysine-Modified Myofibrillar Protein Emulsions |
| title_full_unstemmed | 3D Printability of Lysine-Modified Myofibrillar Protein Emulsions |
| title_short | 3D Printability of Lysine-Modified Myofibrillar Protein Emulsions |
| title_sort | 3d printability of lysine modified myofibrillar protein emulsions |
| topic | lysine myofibrillar protein HIPEs 3D printability |
| url | https://www.mdpi.com/2304-8158/14/12/2138 |
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