Structural Characterization, Technofunctional and Rheological Properties of Sesame Proteins Treated by High-Intensity Ultrasound
Plant-derived proteins, such as those from sesame seeds, have the potential to be used as versatile food ingredients. End-use functionality can be further improved by high-intensity ultrasound treatments. The effects of high-intensity ultrasound on the properties of sesame protein isolates from cold...
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MDPI AG
2023-04-01
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author | Osman Gul Furkan Turker Saricaoglu Ilyas Atalar Latife Betul Gul Fatih Tornuk Senay Simsek |
author_facet | Osman Gul Furkan Turker Saricaoglu Ilyas Atalar Latife Betul Gul Fatih Tornuk Senay Simsek |
author_sort | Osman Gul |
collection | DOAJ |
description | Plant-derived proteins, such as those from sesame seeds, have the potential to be used as versatile food ingredients. End-use functionality can be further improved by high-intensity ultrasound treatments. The effects of high-intensity ultrasound on the properties of sesame protein isolates from cold-pressed sesame cake were evaluated. The SDS-PAGE demonstrated no significant changes in the molecular weight of proteins. Ultrasound treatments resulted in decreased particle size with a more uniform distribution, resulting in the exposure of hydrophobicity and free −SH groups and increased zeta potential. Although FTIR spectra of proteins were similar after ultrasonication, a partial increase in the intensity of the amide A band was observed. The ultrasound significantly (<i>p</i> < 0.05) affected the secondary structure of proteins. While optical micrographics revealed a dispersed structure with smaller particles after treatments, microstructural observations indicated more rough and irregular surfaces. Water solubility was improved to 80.73% in the sample subjected to 6 min of ultrasonication. Sesame protein solutions treated for 4 and 6 min exhibited viscoelastic structure (storage modulus (G′) > loss modulus (G′′)). In addition, the gelation temperature of proteins decreased to about 60–65 °C with increasing treatment time. Overall, ultrasound is a useful technique for the modification of sesame protein isolates. |
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language | English |
last_indexed | 2024-03-11T04:19:04Z |
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spelling | doaj.art-43240506ff0846ada6bb47a4c8f03a802023-11-17T22:54:54ZengMDPI AGFoods2304-81582023-04-01129179110.3390/foods12091791Structural Characterization, Technofunctional and Rheological Properties of Sesame Proteins Treated by High-Intensity UltrasoundOsman Gul0Furkan Turker Saricaoglu1Ilyas Atalar2Latife Betul Gul3Fatih Tornuk4Senay Simsek5Department of Food Engineering, Faculty of Engineering and Architecture, Kastamonu University, 37150 Kastamonu, TurkeyDepartment of Food Engineering, Faculty of Engineering and Natural Sciences, Bursa Technical University, 16310 Bursa, TurkeyDepartment of Food Engineering, Faculty of Agriculture, Eskisehir Osmangazi University, 26160 Eskisehir, TurkeyDepartment of Food Engineering, Faculty of Engineering, Giresun University, 28200 Giresun, TurkeyDepartment of Food Engineering, Faculty of Chemical and Metallurgical Engineering, Yildiz Technical University, 34349 Istanbul, TurkeyDepartment of Food Science & Whistler Center for Carbohydrate Research, Purdue University, West Lafayette, IN 47907, USAPlant-derived proteins, such as those from sesame seeds, have the potential to be used as versatile food ingredients. End-use functionality can be further improved by high-intensity ultrasound treatments. The effects of high-intensity ultrasound on the properties of sesame protein isolates from cold-pressed sesame cake were evaluated. The SDS-PAGE demonstrated no significant changes in the molecular weight of proteins. Ultrasound treatments resulted in decreased particle size with a more uniform distribution, resulting in the exposure of hydrophobicity and free −SH groups and increased zeta potential. Although FTIR spectra of proteins were similar after ultrasonication, a partial increase in the intensity of the amide A band was observed. The ultrasound significantly (<i>p</i> < 0.05) affected the secondary structure of proteins. While optical micrographics revealed a dispersed structure with smaller particles after treatments, microstructural observations indicated more rough and irregular surfaces. Water solubility was improved to 80.73% in the sample subjected to 6 min of ultrasonication. Sesame protein solutions treated for 4 and 6 min exhibited viscoelastic structure (storage modulus (G′) > loss modulus (G′′)). In addition, the gelation temperature of proteins decreased to about 60–65 °C with increasing treatment time. Overall, ultrasound is a useful technique for the modification of sesame protein isolates.https://www.mdpi.com/2304-8158/12/9/1791sesame proteinhigh-intensity ultrasoundtechnofunctional propertiesstructural propertiesrheological properties |
spellingShingle | Osman Gul Furkan Turker Saricaoglu Ilyas Atalar Latife Betul Gul Fatih Tornuk Senay Simsek Structural Characterization, Technofunctional and Rheological Properties of Sesame Proteins Treated by High-Intensity Ultrasound Foods sesame protein high-intensity ultrasound technofunctional properties structural properties rheological properties |
title | Structural Characterization, Technofunctional and Rheological Properties of Sesame Proteins Treated by High-Intensity Ultrasound |
title_full | Structural Characterization, Technofunctional and Rheological Properties of Sesame Proteins Treated by High-Intensity Ultrasound |
title_fullStr | Structural Characterization, Technofunctional and Rheological Properties of Sesame Proteins Treated by High-Intensity Ultrasound |
title_full_unstemmed | Structural Characterization, Technofunctional and Rheological Properties of Sesame Proteins Treated by High-Intensity Ultrasound |
title_short | Structural Characterization, Technofunctional and Rheological Properties of Sesame Proteins Treated by High-Intensity Ultrasound |
title_sort | structural characterization technofunctional and rheological properties of sesame proteins treated by high intensity ultrasound |
topic | sesame protein high-intensity ultrasound technofunctional properties structural properties rheological properties |
url | https://www.mdpi.com/2304-8158/12/9/1791 |
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