Determination and Analysis of Composition, Structure, and Properties of Teff Protein Fractions
To develop teff-based food products with acceptable quality, the composition, structure, and properties of teff protein fractions should be better understood. In this study, teff proteins were extracted, and their protein composition, structure, and properties were calculated, analyzed, and compared...
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| Format: | Article |
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MDPI AG
2023-10-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/12/21/3965 |
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| author | Zhenyang Quan Lili Zhang Wenping Chang Xiangli Ding Jianya Qian Jianhua Tang |
| author_facet | Zhenyang Quan Lili Zhang Wenping Chang Xiangli Ding Jianya Qian Jianhua Tang |
| author_sort | Zhenyang Quan |
| collection | DOAJ |
| description | To develop teff-based food products with acceptable quality, the composition, structure, and properties of teff protein fractions should be better understood. In this study, teff proteins were extracted, and their protein composition, structure, and properties were calculated, analyzed, and compared with those of wheat gliadin and glutenin. Results showed that teff flour contained 9.07% protein, with prolamin as its main protein fraction. The isoelectric points of albumin, globulin, prolamin, and glutelin were at pH 3.6, 3.0, 4.4, and 3.4, respectively. Teff prolamin and glutelin showed a significant difference in amino acids and free energy of hydration compared to wheat gliadins and glutenins. The protein chain length of teff prolamins was smaller than that of wheat gliadins, and teff glutelins lacked high molecular weight glutelin subunits. Teff prolamin had the highest α-helices content (27.08%), whereas no random coils were determined, which is different from wheat gliadin. Teff glutelin had a lower content of β-turn than wheat glutenin, and no α-helices were determined in it. Teff prolamin and glutelin had lower disulfide bond content and surface hydrophobicity. Teff prolamin had significantly higher thermal stability than wheat gliadin, whereas the thermal stability of teff glutelin was significantly lower than that of wheat glutenin. |
| first_indexed | 2024-03-11T11:29:20Z |
| format | Article |
| id | doaj.art-0731316774e346ad9afe7e21a5c30ea4 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-11T11:29:20Z |
| publishDate | 2023-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-0731316774e346ad9afe7e21a5c30ea42023-11-10T15:02:54ZengMDPI AGFoods2304-81582023-10-011221396510.3390/foods12213965Determination and Analysis of Composition, Structure, and Properties of Teff Protein FractionsZhenyang Quan0Lili Zhang1Wenping Chang2Xiangli Ding3Jianya Qian4Jianhua Tang5School of Tourism and Culinary Science, Yangzhou University, Huayang Xilu 196, Yangzhou 225127, ChinaSchool of Food Science and Engineering, Yangzhou University, Huayang Xilu 196, Yangzhou 225127, ChinaSchool of Tourism and Culinary Science, Yangzhou University, Huayang Xilu 196, Yangzhou 225127, ChinaSchool of Tourism and Culinary Science, Yangzhou University, Huayang Xilu 196, Yangzhou 225127, ChinaSchool of Food Science and Engineering, Yangzhou University, Huayang Xilu 196, Yangzhou 225127, ChinaSchool of Tourism and Culinary Science, Yangzhou University, Huayang Xilu 196, Yangzhou 225127, ChinaTo develop teff-based food products with acceptable quality, the composition, structure, and properties of teff protein fractions should be better understood. In this study, teff proteins were extracted, and their protein composition, structure, and properties were calculated, analyzed, and compared with those of wheat gliadin and glutenin. Results showed that teff flour contained 9.07% protein, with prolamin as its main protein fraction. The isoelectric points of albumin, globulin, prolamin, and glutelin were at pH 3.6, 3.0, 4.4, and 3.4, respectively. Teff prolamin and glutelin showed a significant difference in amino acids and free energy of hydration compared to wheat gliadins and glutenins. The protein chain length of teff prolamins was smaller than that of wheat gliadins, and teff glutelins lacked high molecular weight glutelin subunits. Teff prolamin had the highest α-helices content (27.08%), whereas no random coils were determined, which is different from wheat gliadin. Teff glutelin had a lower content of β-turn than wheat glutenin, and no α-helices were determined in it. Teff prolamin and glutelin had lower disulfide bond content and surface hydrophobicity. Teff prolamin had significantly higher thermal stability than wheat gliadin, whereas the thermal stability of teff glutelin was significantly lower than that of wheat glutenin.https://www.mdpi.com/2304-8158/12/21/3965teffprotein fractionscompositionstructureproperties |
| spellingShingle | Zhenyang Quan Lili Zhang Wenping Chang Xiangli Ding Jianya Qian Jianhua Tang Determination and Analysis of Composition, Structure, and Properties of Teff Protein Fractions Foods teff protein fractions composition structure properties |
| title | Determination and Analysis of Composition, Structure, and Properties of Teff Protein Fractions |
| title_full | Determination and Analysis of Composition, Structure, and Properties of Teff Protein Fractions |
| title_fullStr | Determination and Analysis of Composition, Structure, and Properties of Teff Protein Fractions |
| title_full_unstemmed | Determination and Analysis of Composition, Structure, and Properties of Teff Protein Fractions |
| title_short | Determination and Analysis of Composition, Structure, and Properties of Teff Protein Fractions |
| title_sort | determination and analysis of composition structure and properties of teff protein fractions |
| topic | teff protein fractions composition structure properties |
| url | https://www.mdpi.com/2304-8158/12/21/3965 |
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