Structural Characterization and Evaluation of Interfacial Properties of Pea Protein Isolate–EGCG Molecular Complexes
There is increasing interest in using plant-derived proteins in foods and beverages for environmental, health, and ethical reasons. However, the inherent physicochemical properties and functional performance of many plant proteins limit their widespread application. Here, we prepared pea protein iso...
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MDPI AG
2022-09-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/11/18/2895 |
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| author | Shuang Han Fengzhan Cui David Julian McClements Xingfeng Xu Cuicui Ma Yutang Wang Xuebo Liu Fuguo Liu |
| author_facet | Shuang Han Fengzhan Cui David Julian McClements Xingfeng Xu Cuicui Ma Yutang Wang Xuebo Liu Fuguo Liu |
| author_sort | Shuang Han |
| collection | DOAJ |
| description | There is increasing interest in using plant-derived proteins in foods and beverages for environmental, health, and ethical reasons. However, the inherent physicochemical properties and functional performance of many plant proteins limit their widespread application. Here, we prepared pea protein isolate (PPI) dispersions using a combined pH-shift/heat treatment method, and then, prepared PPI-epigallocatechin-3-gallate (EGCG) complexes under neutral conditions. Spectroscopy, calorimetry, molecular docking, and light scattering analysis demonstrated that the molecular complexes formed spontaneously. This was primarily ascribed to hydrogen bonds and van der Waals forces. The complexation of EGCG caused changes in the secondary structure of PPI, including the reduction in the α-helix and increase in the β-sheet and disordered regions. These changes slightly decreased the thermal stability of the protein. With the accretion of EGCG, the hydrophilicity of the complexes increased significantly, which improved the functional attributes of the protein. Optimization of the PPI-to-EGCG ratio led to the complexes having better foaming and emulsifying properties than the protein alone. This study could broaden the utilization of pea proteins as functional ingredients in foods. Moreover, protein–polyphenol complexes can be used as multifunctional ingredients, such as antioxidants or nutraceutical emulsifiers. |
| first_indexed | 2024-03-10T00:02:41Z |
| format | Article |
| id | doaj.art-c53a2483e143458b86b72339182e0785 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-10T00:02:41Z |
| publishDate | 2022-09-01 |
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| series | Foods |
| spelling | doaj.art-c53a2483e143458b86b72339182e07852023-11-23T16:15:02ZengMDPI AGFoods2304-81582022-09-011118289510.3390/foods11182895Structural Characterization and Evaluation of Interfacial Properties of Pea Protein Isolate–EGCG Molecular ComplexesShuang Han0Fengzhan Cui1David Julian McClements2Xingfeng Xu3Cuicui Ma4Yutang Wang5Xuebo Liu6Fuguo Liu7College of Food Science and Engineering, Northwest A&F University, Xianyang 712100, ChinaCollege of Food Science and Engineering, Northwest A&F University, Xianyang 712100, ChinaDepartment of Food Science, University of Massachusetts Amherst, Amherst, MA 01003, USACollege of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, ChinaCollege of Food Science and Engineering, Northwest A&F University, Xianyang 712100, ChinaCollege of Food Science and Engineering, Northwest A&F University, Xianyang 712100, ChinaCollege of Food Science and Engineering, Northwest A&F University, Xianyang 712100, ChinaCollege of Food Science and Engineering, Northwest A&F University, Xianyang 712100, ChinaThere is increasing interest in using plant-derived proteins in foods and beverages for environmental, health, and ethical reasons. However, the inherent physicochemical properties and functional performance of many plant proteins limit their widespread application. Here, we prepared pea protein isolate (PPI) dispersions using a combined pH-shift/heat treatment method, and then, prepared PPI-epigallocatechin-3-gallate (EGCG) complexes under neutral conditions. Spectroscopy, calorimetry, molecular docking, and light scattering analysis demonstrated that the molecular complexes formed spontaneously. This was primarily ascribed to hydrogen bonds and van der Waals forces. The complexation of EGCG caused changes in the secondary structure of PPI, including the reduction in the α-helix and increase in the β-sheet and disordered regions. These changes slightly decreased the thermal stability of the protein. With the accretion of EGCG, the hydrophilicity of the complexes increased significantly, which improved the functional attributes of the protein. Optimization of the PPI-to-EGCG ratio led to the complexes having better foaming and emulsifying properties than the protein alone. This study could broaden the utilization of pea proteins as functional ingredients in foods. Moreover, protein–polyphenol complexes can be used as multifunctional ingredients, such as antioxidants or nutraceutical emulsifiers.https://www.mdpi.com/2304-8158/11/18/2895pea protein isolateEGCGinteractioninterfacial properties |
| spellingShingle | Shuang Han Fengzhan Cui David Julian McClements Xingfeng Xu Cuicui Ma Yutang Wang Xuebo Liu Fuguo Liu Structural Characterization and Evaluation of Interfacial Properties of Pea Protein Isolate–EGCG Molecular Complexes Foods pea protein isolate EGCG interaction interfacial properties |
| title | Structural Characterization and Evaluation of Interfacial Properties of Pea Protein Isolate–EGCG Molecular Complexes |
| title_full | Structural Characterization and Evaluation of Interfacial Properties of Pea Protein Isolate–EGCG Molecular Complexes |
| title_fullStr | Structural Characterization and Evaluation of Interfacial Properties of Pea Protein Isolate–EGCG Molecular Complexes |
| title_full_unstemmed | Structural Characterization and Evaluation of Interfacial Properties of Pea Protein Isolate–EGCG Molecular Complexes |
| title_short | Structural Characterization and Evaluation of Interfacial Properties of Pea Protein Isolate–EGCG Molecular Complexes |
| title_sort | structural characterization and evaluation of interfacial properties of pea protein isolate egcg molecular complexes |
| topic | pea protein isolate EGCG interaction interfacial properties |
| url | https://www.mdpi.com/2304-8158/11/18/2895 |
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