Gul, Osman, Saricaoglu, Furkan Turker, Atalar, Ilyas, Gul, Latife Betul, Tornuk, Fatih, Simsek, SenayGul O., Saricaoglu F.T., Atalar I., Gul L.B., Tornuk F., Simsek S.Gul, O, Saricaoglu, FT, Atalar, I, Gul, LB, Tornuk, F, Simsek, S2023-06-172023-06-172023-04-262023-05-012023.01.01https://hdl.handle.net/20.500.12597/15873Plant-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 ( < 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.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 (p < 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.truehigh-intensity ultrasoundrheological propertiessesame proteinstructural propertiestechnofunctional propertieshigh-intensity ultrasound | rheological properties | sesame protein | structural properties | technofunctional propertiesJournal Article10.3390/foods1209179110.3390/foods120917912-s2.0-85159223844WOS:00098667970000137174329122304-8158