Structural Characterization, Technofunctional and Rheological Properties of Sesame Proteins Treated by High-Intensity Ultrasound
| dc.authorid | 0000-0003-1173-5793 | |
| dc.authorid | 0000-0003-0238-5947 | |
| dc.authorid | 0000-0001-8560-0010 | |
| dc.authorid | 0000-0002-7313-0207 | |
| dc.authorid | 0000-0003-1620-4246 | |
| dc.authorid | 0000-0002-4732-7727 | |
| dc.contributor.author | Gul, Osman | |
| dc.contributor.author | Saricaoglu, Furkan Turker | |
| dc.contributor.author | Atalar, Ilyas | |
| dc.contributor.author | Gul, Latife Betul | |
| dc.contributor.author | Tornuk, Fatih | |
| dc.contributor.author | Simsek, Senay | |
| dc.date.accessioned | 2026-02-12T21:05:12Z | |
| dc.date.available | 2026-02-12T21:05:12Z | |
| dc.date.issued | 2023 | |
| dc.department | Bursa Teknik Üniversitesi | |
| dc.description.abstract | 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 degrees C with increasing treatment time. Overall, ultrasound is a useful technique for the modification of sesame protein isolates. | |
| dc.description.sponsorship | Turkish Scientific and Technical Research Council (TUBITAK) [TOVAG 120O773] | |
| dc.description.sponsorship | This research was funded by the Turkish Scientific and Technical Research Council (TUBITAK) for the project (Project Number: TOVAG 120O773). | |
| dc.identifier.doi | 10.3390/foods12091791 | |
| dc.identifier.issn | 2304-8158 | |
| dc.identifier.issue | 9 | |
| dc.identifier.pmid | 37174329 | |
| dc.identifier.scopus | 2-s2.0-85159223844 | |
| dc.identifier.scopusquality | Q1 | |
| dc.identifier.uri | https://doi.org/10.3390/foods12091791 | |
| dc.identifier.uri | https://hdl.handle.net/20.500.12885/6848 | |
| dc.identifier.volume | 12 | |
| dc.identifier.wos | WOS:000986679700001 | |
| dc.identifier.wosquality | Q1 | |
| dc.indekslendigikaynak | Web of Science | |
| dc.indekslendigikaynak | Scopus | |
| dc.indekslendigikaynak | PubMed | |
| dc.language.iso | en | |
| dc.publisher | Mdpi | |
| dc.relation.ispartof | Foods | |
| dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.snmz | KA_WoS_20260212 | |
| dc.subject | sesame protein | |
| dc.subject | high-intensity ultrasound | |
| dc.subject | technofunctional properties | |
| dc.subject | structural properties | |
| dc.subject | rheological properties | |
| dc.title | Structural Characterization, Technofunctional and Rheological Properties of Sesame Proteins Treated by High-Intensity Ultrasound | |
| dc.type | Article |












