Molecular insights into the structure forming properties of zein and a rheological comparison with hordein
Prolamins are hydrophobic proteins extracted using water-ethanol mixtures, useful for texturing meat and cheese alternatives at low temperatures due to their self-aggregating properties. This study explored the rheological and structural properties of the corn prolamin zein under varying temperature...
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| Format: | Article |
| Language: | English |
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Elsevier
2024-12-01
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| Series: | Future Foods |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2666833524002077 |
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| author | Bhanu Devnani Nicholle Kirsten Tan Jeffrey M Sanders John C Shelley Francesca Moraca Lutz Grossmann |
| author_facet | Bhanu Devnani Nicholle Kirsten Tan Jeffrey M Sanders John C Shelley Francesca Moraca Lutz Grossmann |
| author_sort | Bhanu Devnani |
| collection | DOAJ |
| description | Prolamins are hydrophobic proteins extracted using water-ethanol mixtures, useful for texturing meat and cheese alternatives at low temperatures due to their self-aggregating properties. This study explored the rheological and structural properties of the corn prolamin zein under varying temperature and pH conditions and compared its rheological behavior to the barley prolamin hordein. Zein showed plasticization when heated, with plasticization temperatures ranging from 41.3 °C at pH 4 to 46.7 °C at pH 6. Texture maps indicated that zein formed brittle gels within the linear viscoelastic range and tougher structures at crossover, unlike hordein, which was more elastic and lacked a clear plasticization behavior (softening) during heating. These differences were linked to zein's hydrophobicity. Coarse-grained molecular dynamics simulations showed zein self-aligning into anisotropic protein structures during heating, with its radius of gyration increasing from Rg = 21 Å to Rg = 34 Å by heating. This study provided insights into the structuring of prolamins and highlighted the need to understand plasticization mechanisms to improve zein's functionality in food applications. |
| format | Article |
| id | doaj-art-edcb4c97296d40a694d6be9b49a9edb8 |
| institution | Kabale University |
| issn | 2666-8335 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Future Foods |
| spelling | doaj-art-edcb4c97296d40a694d6be9b49a9edb82024-12-18T08:53:57ZengElsevierFuture Foods2666-83352024-12-0110100503Molecular insights into the structure forming properties of zein and a rheological comparison with hordeinBhanu Devnani0Nicholle Kirsten Tan1Jeffrey M Sanders2John C Shelley3Francesca Moraca4Lutz Grossmann5Department of Food Science, University of Massachusetts, 100 Holdsworth Way, Amherst, MA 01003, USADepartment of Food Science, University of Massachusetts, 100 Holdsworth Way, Amherst, MA 01003, USADepartment of Food Science, University of Massachusetts, 100 Holdsworth Way, Amherst, MA 01003, USA; Schrödinger Inc, 1540 Broadway 24th Floor, New York, NY 10036, USASchrödinger Inc, 1540 Broadway 24th Floor, New York, NY 10036, USASchrödinger Inc, 1540 Broadway 24th Floor, New York, NY 10036, USADepartment of Food Science, University of Massachusetts, 100 Holdsworth Way, Amherst, MA 01003, USA; Corresponding author.Prolamins are hydrophobic proteins extracted using water-ethanol mixtures, useful for texturing meat and cheese alternatives at low temperatures due to their self-aggregating properties. This study explored the rheological and structural properties of the corn prolamin zein under varying temperature and pH conditions and compared its rheological behavior to the barley prolamin hordein. Zein showed plasticization when heated, with plasticization temperatures ranging from 41.3 °C at pH 4 to 46.7 °C at pH 6. Texture maps indicated that zein formed brittle gels within the linear viscoelastic range and tougher structures at crossover, unlike hordein, which was more elastic and lacked a clear plasticization behavior (softening) during heating. These differences were linked to zein's hydrophobicity. Coarse-grained molecular dynamics simulations showed zein self-aligning into anisotropic protein structures during heating, with its radius of gyration increasing from Rg = 21 Å to Rg = 34 Å by heating. This study provided insights into the structuring of prolamins and highlighted the need to understand plasticization mechanisms to improve zein's functionality in food applications.http://www.sciencedirect.com/science/article/pii/S2666833524002077Corn proteinMD simulationAlternative proteinSustainable proteinExtrusion |
| spellingShingle | Bhanu Devnani Nicholle Kirsten Tan Jeffrey M Sanders John C Shelley Francesca Moraca Lutz Grossmann Molecular insights into the structure forming properties of zein and a rheological comparison with hordein Future Foods Corn protein MD simulation Alternative protein Sustainable protein Extrusion |
| title | Molecular insights into the structure forming properties of zein and a rheological comparison with hordein |
| title_full | Molecular insights into the structure forming properties of zein and a rheological comparison with hordein |
| title_fullStr | Molecular insights into the structure forming properties of zein and a rheological comparison with hordein |
| title_full_unstemmed | Molecular insights into the structure forming properties of zein and a rheological comparison with hordein |
| title_short | Molecular insights into the structure forming properties of zein and a rheological comparison with hordein |
| title_sort | molecular insights into the structure forming properties of zein and a rheological comparison with hordein |
| topic | Corn protein MD simulation Alternative protein Sustainable protein Extrusion |
| url | http://www.sciencedirect.com/science/article/pii/S2666833524002077 |
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