Fibrillisation of faba bean protein isolate by thermosonication for process efficacy: Microstructural characteristics, assembly behaviour, and physicochemical properties

Simple item page
dc.citation.volume154
dc.contributor.authorHu Y
dc.contributor.authorCheng L
dc.contributor.authorGilbert EP
dc.contributor.authorLoo TS
dc.contributor.authorLee SJ
dc.contributor.authorHarrison J
dc.contributor.authorYang Z
dc.date.accessioned2024-05-15T02:46:05Z
dc.date.available2024-05-15T02:46:05Z
dc.date.issued2024-09
dc.description.abstractThe effect of thermosonication (TS) (90 °C, 10–30 min) on the fibrillisation of faba bean protein isolate (FPI) was studied. The self-assembly behaviour, microstructural characteristics and techno-functional (gelation and emulsification) properties of FPI fibrils obtained from TS treatment were compared with those obtained from conventional prolonged heating (CH) at 90 °C up to 8 h. Compared to CH treatment, TS treatment was shown to significantly accelerate the formation of FPI fibrils with prominent β-sheet structures as revealed by Thioflavin T (ThT) fluorescence, Fourier-transform infrared spectroscopy (FTIR) and circular dichroism (CD). The characteristics of fibril building blocks were analysed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and liquid chromatography linked to tandem mass spectrometry (LC-MS/MS) to obtain the differences between TS and CH induced fibrillisation of FPI. Transmission electron microscopy (TEM) and small-angle neutron scattering (SANS) showed that 4 h CH and 10 min TS treatments resulted in the fibrils with similar radius (from 5 to 10 nm). Furthermore, SANS indicated that TS treatment induced the formation of an entangled FPI fibrillar network, which could lead to the observed viscoelastic properties of FPI at a high concentration (10 wt%). Finally, high internal phase O/W emulsions (HIPE, φ = 0.75) stabilised by 30 min TS induced FPI fibrils (3 wt%) demonstrated a stronger gel strength and smaller oil droplet size compared to those prepared with untreated FPI, suggesting a superior emulsification capability of FPI fibrils. This finding demonstrates that TS treatment is a promising and efficient method for fibrillisation of plant proteins with the resultant fibrils generating excellent gelation and emulsification properties.
dc.description.confidentialfalse
dc.edition.editionSeptember 2024
dc.identifier.citationHu Y, Cheng L, Gilbert EP, Loo TS, Lee SJ, Harrison J, Yang Z. (2024). Fibrillisation of faba bean protein isolate by thermosonication for process efficacy: Microstructural characteristics, assembly behaviour, and physicochemical properties. Food Hydrocolloids. 154.
dc.identifier.doi10.1016/j.foodhyd.2024.110127
dc.identifier.eissn1873-7137
dc.identifier.elements-typejournal-article
dc.identifier.issn0268-005X
dc.identifier.number110127
dc.identifier.piiS0268005X24004016
dc.identifier.urihttps://mro.massey.ac.nz/handle/10179/69568
dc.languageEnglish
dc.publisherElsevier Ltd
dc.publisher.urihttps://www.sciencedirect.com/science/article/pii/S0268005X24004016
dc.relation.isPartOfFood Hydrocolloids
dc.rights(c) 2024 The Author/s
dc.rightsCC BY-NC 4.0
dc.rights.urihttps://creativecommons.org/licenses/by-nc/4.0/
dc.subjectThermosonication
dc.subjectSelf-assembly fibrils
dc.subjectFaba bean protein isolates
dc.subjectSmall angle neutron scattering
dc.subjectHigh internal phase emulsions
dc.subjectMicrostructures
dc.titleFibrillisation of faba bean protein isolate by thermosonication for process efficacy: Microstructural characteristics, assembly behaviour, and physicochemical properties
dc.typeJournal article
pubs.elements-id488522
pubs.organisational-groupOther
Files
Original bundle
Now showing 1 - 2 of 2
Thumbnail Image
Name:
Published version.pdf
Size:
10.8 MB
Format:
Adobe Portable Document Format
Description:
488522 PDF.pdf
Download
Thumbnail Image
Name:
Evidence.xml
Size:
1.26 MB
Format:
Extensible Markup Language
Description:
1-s2.0-S0268005X24004016-mmc1.docx
Download
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
9.22 KB
Format:
Plain Text
Description:
Download
Collections
Journal Articles