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Authordc.contributor.authorVera, A. 
Authordc.contributor.authorValenzuela, M. A. 
Authordc.contributor.authorYazdani-Pedram Zobeiri, Mehrdad 
Authordc.contributor.authorTapia, C. 
Authordc.contributor.authorAbugoch James, Lilian 
Admission datedc.date.accessioned2019-05-31T15:34:02Z
Available datedc.date.available2019-05-31T15:34:02Z
Publication datedc.date.issued2019
Cita de ítemdc.identifier.citationUltrasonics - Sonochemistry 51 (2019) 186–196
Identifierdc.identifier.issn18732828
Identifierdc.identifier.issn13504177
Identifierdc.identifier.other10.1016/j.ultsonch.2018.10.026
Identifierdc.identifier.urihttps://repositorio.uchile.cl/handle/2250/169710
Abstractdc.description.abstractQuinoa proteins (QP) have promise as a potential source of novel food ingredients, and it is of great interest to know how high-intensity ultrasound (HIUS) treatments affect the properties of QP. This work aimed to study the impact of on-off time-pulses of HIUS treatments on the structural and physicochemical properties of QP; samples were treated at 5, 10, 20, and 30 min with on-off pulses of 10s/10s, 5s/1s, and 1s/5s). Structural changes were evaluated using PAGE-SDS, circular dichroism, fluorescence spectroscopy, and differential scanning calorimetry. Meanwhile, physicochemical properties were also examined, including solubility, Z-average, polydispersity index PDI, and Z-potential. PAGE-SDS showed the appearance of polypeptides over 190 kDa in HIUS samples treated. All samples presented 15.6% alpha-helices, 31.3% beta-sheets, 21.8% beta-rotations, and 31.4% random coils independent of the HIUS treatment. beta-Turn structures and "random coils" were not affected by HIUS. When US 10s/10s and 1s/5s were applied, an increase in the % alpha-helix and a decrease in beta-fold were observed, which could indicate a small conversion of beta-folds to alpha-helices. Fluorescence spectra for all HIUS showed a significant increase (23%) of average fluorescence intensity and a decrease of lambda max in relation to that of the control (346 dnm and 340 nm average HIUS treatment). DSC showed one endotherm in all cases (81.6-99.8 degrees C), and an increase in Td was observed due to the effect of the HIUS treatment. HIUS caused a 48% increase in solubility. The Z-average of the HIUS samples compared to that of the controls showed an increase from 37.8 to 47.3 nm. PDI and Z-potential values from the QP controls and the HIUS samples did not show significance differences and presented average values of 0.466 +/- 0.021 (PDI) and - 16.63 +/- 0.89 (Z-potential). It is possible to conclude that HIUS treatments affect the secondary and tertiary structure of quinoa proteins, and these changes resulted in an increase of solubility and particle size. HIUS treatment as a new and promising technology that can improve the QP solubility properties and in that way allow its use as an ingredient with a good source of protein to develop different types of beverages/protein sauces.
Lenguagedc.language.isoen
Publisherdc.publisherElsevier
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
Link to Licensedc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
Sourcedc.sourceUltrasonics Sonochemistry
Keywordsdc.subjectConformational structure
Keywordsdc.subjectHigh-intensity ultrasound
Keywordsdc.subjectPhysicochemical properties
Keywordsdc.subjectPulses on-off
Keywordsdc.subjectQuinoa proteins
Títulodc.titleConformational and physicochemical properties of quinoa proteins affected by different conditions of high-intensity ultrasound treatments
Document typedc.typeArtículo de revista
Catalogueruchile.catalogadorlaj
Indexationuchile.indexArtículo de publicación SCOPUS
uchile.cosechauchile.cosechaSI


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Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile