Truncated protein extraction modulates pea protein–carbohydrate thermal co-gelation
(2026) In Food Hydrocolloids 177.- Abstract
- Conventional methods of pea protein extraction are resource-intensive,
involving multiple purification steps that remove co-existing components
such as starch. In contrast, we investigate how minimally processed
yellow pea protein extracts that retain residual carbohydrates form
thermally induced gels. Contrast-variation small-angle neutron
scattering, rheology, and differential scanning calorimetry show that
salt-extracted samples form a unified gel matrix through co-gelation of
protein and carbohydrate components, as evidenced by a shared contrast
match point in the final network. Ultra-small-angle neutron scattering
reveals mesoscale heterogeneity, with structural features persisting up
... (More) - Conventional methods of pea protein extraction are resource-intensive,
involving multiple purification steps that remove co-existing components
such as starch. In contrast, we investigate how minimally processed
yellow pea protein extracts that retain residual carbohydrates form
thermally induced gels. Contrast-variation small-angle neutron
scattering, rheology, and differential scanning calorimetry show that
salt-extracted samples form a unified gel matrix through co-gelation of
protein and carbohydrate components, as evidenced by a shared contrast
match point in the final network. Ultra-small-angle neutron scattering
reveals mesoscale heterogeneity, with structural features persisting up
to 2 μm,
indicative of a particulate, protein-rich network within the composite
gel. Rheological and calorimetric analyses suggest that gelation
proceeds via a kinetic pathway in which protein aggregation precedes
unfolding, ultimately shaping network architecture and viscoelastic
properties. These findings demonstrate that minimal processing can yield
structurally integrated protein–starch gels and clarify how composition
and processing determine network architecture and mechanical
performance. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/c1c9414a-c7e5-472d-8fc1-60344964b6e0
- author
- Francis, Juanita LU ; Dessì, Francesca LU ; Jackson, Andrew LU ; Gilbert, Elliot P. ; Mata, Jitendra P. ; Schirone, Davide LU and Roosen-Runge, Felix LU
- organization
- publishing date
- 2026-02
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Food Hydrocolloids
- volume
- 177
- article number
- 112555
- pages
- 11 pages
- publisher
- Elsevier
- ISSN
- 0268-005X
- DOI
- 10.1016/j.foodhyd.2026.112555
- language
- English
- LU publication?
- yes
- id
- c1c9414a-c7e5-472d-8fc1-60344964b6e0
- date added to LUP
- 2026-03-03 11:39:19
- date last changed
- 2026-03-06 13:33:24
@article{c1c9414a-c7e5-472d-8fc1-60344964b6e0,
abstract = {{Conventional methods of pea protein extraction are resource-intensive, <br>
involving multiple purification steps that remove co-existing components<br>
such as starch. In contrast, we investigate how minimally processed <br>
yellow pea protein extracts that retain residual carbohydrates form <br>
thermally induced gels. Contrast-variation small-angle neutron <br>
scattering, rheology, and differential scanning calorimetry show that <br>
salt-extracted samples form a unified gel matrix through co-gelation of <br>
protein and carbohydrate components, as evidenced by a shared contrast <br>
match point in the final network. Ultra-small-angle neutron scattering <br>
reveals mesoscale heterogeneity, with structural features persisting up <br>
to 2 μm,<br>
indicative of a particulate, protein-rich network within the composite <br>
gel. Rheological and calorimetric analyses suggest that gelation <br>
proceeds via a kinetic pathway in which protein aggregation precedes <br>
unfolding, ultimately shaping network architecture and viscoelastic <br>
properties. These findings demonstrate that minimal processing can yield<br>
structurally integrated protein–starch gels and clarify how composition<br>
and processing determine network architecture and mechanical <br>
performance.}},
author = {{Francis, Juanita and Dessì, Francesca and Jackson, Andrew and Gilbert, Elliot P. and Mata, Jitendra P. and Schirone, Davide and Roosen-Runge, Felix}},
issn = {{0268-005X}},
language = {{eng}},
publisher = {{Elsevier}},
series = {{Food Hydrocolloids}},
title = {{Truncated protein extraction modulates pea protein–carbohydrate thermal co-gelation}},
url = {{http://dx.doi.org/10.1016/j.foodhyd.2026.112555}},
doi = {{10.1016/j.foodhyd.2026.112555}},
volume = {{177}},
year = {{2026}},
}