Yayın: Structural Characterization, Technofunctional and Rheological Properties of Sesame Proteins Treated by High-Intensity Ultrasound
| 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 | 2026-01-04T18:39:18Z | |
| dc.date.issued | 2023-04-26 | |
| 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 °C with increasing treatment time. Overall, ultrasound is a useful technique for the modification of sesame protein isolates. | |
| dc.description.uri | https://doi.org/10.3390/foods12091791 | |
| dc.description.uri | https://pubmed.ncbi.nlm.nih.gov/37174329 | |
| dc.description.uri | http://dx.doi.org/10.3390/foods12091791 | |
| dc.description.uri | https://doaj.org/article/43240506ff0846ada6bb47a4c8f03a80 | |
| dc.description.uri | https://dx.doi.org/10.3390/foods12091791 | |
| dc.description.uri | https://avesis.yildiz.edu.tr/publication/details/72e41452-66c9-426f-956c-556d507eee36/oai | |
| dc.description.uri | https://aperta.ulakbim.gov.tr/record/267202 | |
| dc.identifier.doi | 10.3390/foods12091791 | |
| dc.identifier.eissn | 2304-8158 | |
| dc.identifier.openaire | doi_dedup___::4dea114f8b46489a23786763cd6325fa | |
| dc.identifier.orcid | 0000-0003-1620-4246 | |
| dc.identifier.orcid | 0000-0003-1173-5793 | |
| dc.identifier.orcid | 0000-0001-8560-0010 | |
| dc.identifier.orcid | 0000-0002-4732-7727 | |
| dc.identifier.orcid | 0000-0002-7313-0207 | |
| dc.identifier.orcid | 0000-0003-0238-5947 | |
| dc.identifier.pubmed | 37174329 | |
| dc.identifier.scopus | 2-s2.0-85159223844 | |
| dc.identifier.startpage | 1791 | |
| dc.identifier.uri | https://hdl.handle.net/20.500.12597/40677 | |
| dc.identifier.volume | 12 | |
| dc.identifier.wos | 000986679700001 | |
| dc.language.iso | eng | |
| dc.publisher | MDPI AG | |
| dc.relation.ispartof | Foods | |
| dc.rights | OPEN | |
| dc.subject | structural properties | |
| dc.subject | rheological properties | |
| dc.subject | Chemical technology | |
| dc.subject | sesame protein | |
| dc.subject | high-intensity ultrasound | |
| dc.subject | technofunctional properties | |
| dc.subject | structural properties | |
| dc.subject | rheological properties | |
| dc.subject | technofunctional properties | |
| dc.subject | high-intensity ultrasound | |
| dc.subject | TP1-1185 | |
| dc.subject | sesame protein | |
| dc.subject | Article | |
| dc.title | Structural Characterization, Technofunctional and Rheological Properties of Sesame Proteins Treated by High-Intensity Ultrasound | |
| dc.type | Article | |
| dspace.entity.type | Publication | |
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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. 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| local.import.source | OpenAire | |
| local.indexed.at | WOS | |
| local.indexed.at | Scopus | |
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