Impacts of sonication and high hydrostatic pressure on the structural and physicochemical properties of quinoa protein isolate dispersions at acidic, neutral and alkaline pHs

dc.citation.volume91
dc.contributor.authorLuo L
dc.contributor.authorYang Z
dc.contributor.authorWang H
dc.contributor.authorMuthupandian A
dc.contributor.authorHemar Y
dc.coverage.spatialNetherlands
dc.date.accessioned2023-10-31T22:20:52Z
dc.date.accessioned2023-11-03T04:45:58Z
dc.date.available2022-11-21
dc.date.available2023-10-31T22:20:52Z
dc.date.available2023-11-03T04:45:58Z
dc.date.issued2022-12
dc.description.abstractHerein, 1 wt% quinoa protein isolate (QPI) was exposed to sonication using a 20 kHz ultrasonicator equipped with a 6 mm horn (14.4 W, 10 mL, up to 15 min) or high hydrostatic pressure (HHP, up to 600 MPa, 15 min) treatments at pH 5, pH 7, and pH 9. The changes to physicochemical properties were probed by SDS-PAGE, FTIR, free sulfhydryl group (SH), surface hydrophobicity (H0), particle size and solubility. As revealed by SDS-PAGE, substantial amounts of 11S globulin participated in the formations of aggregates via Ssingle bondS bond under HHP, particularly at pH 7 and pH 9. However, protein profiles of QPI were not significantly affected by the sonication. Free SH groups and surface hydrophobicity were increased after the sonication treatment indicating protein unfolding and exposure of the embedded SH and/or hydrophobic groups. An opposite trend was observed in HHP treated samples, implying aggregation and reassociation of structures under HHP. HHP and sonication treatments induced a decrease in ordered secondary structures (random coil and β-turn) accompanied with an increase in disordered secondary structures (α-helix and β-sheet) as probed by FTIR. Finally, the sonication treatment induced a significant improvement in the solubility (up to ∼3 folds at pH 7 and ∼2.6 folds at pH 9) and a reduction in particle sizes (up to ∼3 folds at pH 7 and ∼4.4 folds at pH 9). However, HHP treatment (600 MPa) only slightly increased the solubility (∼1.6 folds at pH 7 and ∼1.2 folds at pH 9) and decreased the particle size (∼1.3 folds at pH 7 and ∼1.2 folds at pH 9). This study provides a direct comparison of the impacts of sonication and HHP treatment on QPI, which will enable to choose the appropriate processing methods to achieve tailored properties of QPI.
dc.description.confidentialfalse
dc.edition.editionDecember 2022
dc.format.pagination106232-
dc.identifier.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/36435086
dc.identifier.citationLuo L, Yang Z, Wang H, Ashokkumar M, Hemar Y. (2022). Impacts of sonication and high hydrostatic pressure on the structural and physicochemical properties of quinoa protein isolate dispersions at acidic, neutral and alkaline pHs.. Ultrason Sonochem. 91. (pp. 106232-).
dc.identifier.doi10.1016/j.ultsonch.2022.106232
dc.identifier.eissn1873-2828
dc.identifier.elements-typejournal-article
dc.identifier.issn1350-4177
dc.identifier.number106232
dc.identifier.piiS1350-4177(22)00328-5
dc.identifier.urihttps://mro.massey.ac.nz/handle/10179/68999
dc.languageeng
dc.publisherElsevier BV
dc.publisher.urihttps://www.sciencedirect.com/science/article/pii/S1350417722003285
dc.relation.isPartOfUltrason Sonochem
dc.rights(c) 2022 The Author/s
dc.rightsCC BY-NC-ND 4.0
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectHigh hydrostatic pressure
dc.subjectPhysicochemical properties
dc.subjectQuinoa protein isolates
dc.subjectSonication
dc.subjectChenopodium quinoa
dc.subjectHydrostatic Pressure
dc.titleImpacts of sonication and high hydrostatic pressure on the structural and physicochemical properties of quinoa protein isolate dispersions at acidic, neutral and alkaline pHs
dc.typeJournal article
pubs.elements-id458118
pubs.organisational-groupOther
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