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Structural Characterization, Technofunctional and Rheological Properties of Sesame Proteins Treated by High-Intensity Ultrasound

dc.contributor.authorGul, Osman
dc.contributor.authorSaricaoglu, Furkan Turker
dc.contributor.authorAtalar, Ilyas
dc.contributor.authorGul, Latife Betul
dc.contributor.authorTornuk, Fatih
dc.contributor.authorSimsek, Senay
dc.date.accessioned2026-01-04T18:39:18Z
dc.date.issued2023-04-26
dc.description.abstractPlant-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.urihttps://doi.org/10.3390/foods12091791
dc.description.urihttps://pubmed.ncbi.nlm.nih.gov/37174329
dc.description.urihttp://dx.doi.org/10.3390/foods12091791
dc.description.urihttps://doaj.org/article/43240506ff0846ada6bb47a4c8f03a80
dc.description.urihttps://dx.doi.org/10.3390/foods12091791
dc.description.urihttps://avesis.yildiz.edu.tr/publication/details/72e41452-66c9-426f-956c-556d507eee36/oai
dc.description.urihttps://aperta.ulakbim.gov.tr/record/267202
dc.identifier.doi10.3390/foods12091791
dc.identifier.eissn2304-8158
dc.identifier.openairedoi_dedup___::4dea114f8b46489a23786763cd6325fa
dc.identifier.orcid0000-0003-1620-4246
dc.identifier.orcid0000-0003-1173-5793
dc.identifier.orcid0000-0001-8560-0010
dc.identifier.orcid0000-0002-4732-7727
dc.identifier.orcid0000-0002-7313-0207
dc.identifier.orcid0000-0003-0238-5947
dc.identifier.pubmed37174329
dc.identifier.scopus2-s2.0-85159223844
dc.identifier.startpage1791
dc.identifier.urihttps://hdl.handle.net/20.500.12597/40677
dc.identifier.volume12
dc.identifier.wos000986679700001
dc.language.isoeng
dc.publisherMDPI AG
dc.relation.ispartofFoods
dc.rightsOPEN
dc.subjectstructural properties
dc.subjectrheological properties
dc.subjectChemical technology
dc.subjectsesame protein
dc.subjecthigh-intensity ultrasound
dc.subjecttechnofunctional properties
dc.subjectstructural properties
dc.subjectrheological properties
dc.subjecttechnofunctional properties
dc.subjecthigh-intensity ultrasound
dc.subjectTP1-1185
dc.subjectsesame protein
dc.subjectArticle
dc.titleStructural Characterization, Technofunctional and Rheological Properties of Sesame Proteins Treated by High-Intensity Ultrasound
dc.typeArticle
dspace.entity.typePublication
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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 &lt; 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′) &gt; loss modulus (G′′)). In addition, the gelation temperature of proteins decreased to about 60–65 °C with increasing treatment time. 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