Plant-dairy protein blends: gelation behaviour in a filled particle matrix. (July 2021)
- Record Type:
- Journal Article
- Title:
- Plant-dairy protein blends: gelation behaviour in a filled particle matrix. (July 2021)
- Main Title:
- Plant-dairy protein blends: gelation behaviour in a filled particle matrix
- Authors:
- Grasberger, Katherine Findlay
Gregersen, Sandra Beyer
Jensen, Hanne Bak
Sanggaard, Kristian Wejse
Corredig, Milena - Abstract:
- Graphical abstract: Highlights: All emulsion droplets showed extensive bridging flocculation. Viscosity of the emulsions varied depending on the type of protein added. During heating, structure formation of the mixed systems showed three different stages. Lupin or pea protein isolates with whey protein caused an earlier onset of aggregation. Abstract: The objective of this work was to study the structure formation in mixed protein systems containing oil droplets. A model system was prepared with skim milk, whey proteins and plant proteins to a final concentration of 8% (w/w) and homogenized with 20% (w/w) coconut fat. Three plant-derived protein sources (namely, pea isolate, oat concentrate, and lupin isolate) were added to skim milk at two different ratios of plant/dairy proteins. A blend containing only dairy protein was also used as reference, prepared with skim milk and whey protein isolate. The formation of structure in the emulsion filled gels after homogenization and heating were evaluated, using SDS-PAGE, light scattering, rheology and confocal microscopy. All emulsions showed a high viscosity due to the high extent of bridging flocculation amongst the oil droplets confirmed by a decrease in the particle size of emulsions upon the addition of SDS. After heating and cooling, the emulsions showed no macroscopic phase separation. The results demonstrated that structuring of complex gels can be modulated by controlling the composition at the oil-water interface, as wellGraphical abstract: Highlights: All emulsion droplets showed extensive bridging flocculation. Viscosity of the emulsions varied depending on the type of protein added. During heating, structure formation of the mixed systems showed three different stages. Lupin or pea protein isolates with whey protein caused an earlier onset of aggregation. Abstract: The objective of this work was to study the structure formation in mixed protein systems containing oil droplets. A model system was prepared with skim milk, whey proteins and plant proteins to a final concentration of 8% (w/w) and homogenized with 20% (w/w) coconut fat. Three plant-derived protein sources (namely, pea isolate, oat concentrate, and lupin isolate) were added to skim milk at two different ratios of plant/dairy proteins. A blend containing only dairy protein was also used as reference, prepared with skim milk and whey protein isolate. The formation of structure in the emulsion filled gels after homogenization and heating were evaluated, using SDS-PAGE, light scattering, rheology and confocal microscopy. All emulsions showed a high viscosity due to the high extent of bridging flocculation amongst the oil droplets confirmed by a decrease in the particle size of emulsions upon the addition of SDS. After heating and cooling, the emulsions showed no macroscopic phase separation. The results demonstrated that structuring of complex gels can be modulated by controlling the composition at the oil-water interface, as well as by modulating processing conditions, capitalizing on the gelling properties of the single components in the matrix. … (more)
- Is Part Of:
- Food structure. Volume 29(2021)
- Journal:
- Food structure
- Issue:
- Volume 29(2021)
- Issue Display:
- Volume 29, Issue 2021 (2021)
- Year:
- 2021
- Volume:
- 29
- Issue:
- 2021
- Issue Sort Value:
- 2021-0029-2021-0000
- Page Start:
- Page End:
- Publication Date:
- 2021-07
- Subjects:
- Lupin protein -- Oat protein -- Pea protein -- Whey protein -- Emulsion filled gels
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
Food -- analysis -- Periodicals
Food -- Analysis
Periodicals
664.07 - Journal URLs:
- http://www.sciencedirect.com/science/journal/22133291 ↗
http://www.bibliothek.uni-regensburg.de/ezeit/?2747543 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foostr.2021.100198 ↗
- Languages:
- English
- ISSNs:
- 2213-3291
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 18498.xml