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In-depth exploration of the structure of pea albumin, its fractions and their heating and foaming properties

Li, Ruifen ; Neofytos, Dionysios LU ; Kirkensgaard, Jacob J.K. ; Pal, Antara LU ; Pedersen, Jan Skov and Corredig, Milena LU (2025) In Journal of Colloid and Interface Science 692.
Abstract

Hypothesis: The structure and functionality of pea albumin can be described in detail as a combination of its main fractions, PA1 and PA2. Experimental: PA1 and PA2 were purified from a Pea Albumin extract (PA) using size exclusion chromatography, and characterized by two-dimensional gel electrophoresis. Their secondary structure was analyzed using Fourier-Transform Infrared Spectroscopy (FTIR). The structures before and after heat treatment (90 °C, 1 & 5 min) were investigated by Small-Angle X-ray Scattering (SAXS). SAXS intensities were evaluated using high-resolution models obtained as predictions from the AlphaFold Protein Structure Database. Interfacial and foaming properties were also evaluated. Findings: Both PA1 and PA2... (More)

Hypothesis: The structure and functionality of pea albumin can be described in detail as a combination of its main fractions, PA1 and PA2. Experimental: PA1 and PA2 were purified from a Pea Albumin extract (PA) using size exclusion chromatography, and characterized by two-dimensional gel electrophoresis. Their secondary structure was analyzed using Fourier-Transform Infrared Spectroscopy (FTIR). The structures before and after heat treatment (90 °C, 1 & 5 min) were investigated by Small-Angle X-ray Scattering (SAXS). SAXS intensities were evaluated using high-resolution models obtained as predictions from the AlphaFold Protein Structure Database. Interfacial and foaming properties were also evaluated. Findings: Both PA1 and PA2 contained various isoforms, and PA2 displayed a high β-sheet/α-helix ratio. In solution, SAXS intensities of PA1 could be predicted by its native structure, and after heating PA1 showed limited aggregation. PA2 could be presented as a dimer, which unfolded and formed large aggregates during heating. The high-resolution models could also explain well the SAXS signal of the unfractionated PA, combining PA1 and PA2. After heating, PA2 dominated the properties of the PA mixtures. PA2 predominantly contributed to the interfacial and foaming properties of PA, in spite of both PA1 and PA2 showing adsorption at the air/water interface. Indeed, PA1 in isolation could not form a stable foam. Perspective: SAXS data analyzed with high-resolution structure models allowed for an in depth understanding of the structural changes of PA1 and PA2, and provided a mechanistic understanding of the relationships between structure, composition, and technological functionality of the albumin fractions from pea.

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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Foaming, Heat-induced aggregates, Interfacial properties, PA1, PA2, Pea albumins, SAXS, Secondary structure
in
Journal of Colloid and Interface Science
volume
692
article number
137507
publisher
Academic Press
external identifiers
  • pmid:40188795
  • scopus:105001869729
ISSN
0021-9797
DOI
10.1016/j.jcis.2025.137507
language
English
LU publication?
yes
id
19b8d7b6-7ef3-41fe-ba60-96dbd880ed98
date added to LUP
2025-08-08 08:14:19
date last changed
2025-08-22 09:27:02
@article{19b8d7b6-7ef3-41fe-ba60-96dbd880ed98,
  abstract     = {{<p>Hypothesis: The structure and functionality of pea albumin can be described in detail as a combination of its main fractions, PA1 and PA2. Experimental: PA1 and PA2 were purified from a Pea Albumin extract (PA) using size exclusion chromatography, and characterized by two-dimensional gel electrophoresis. Their secondary structure was analyzed using Fourier-Transform Infrared Spectroscopy (FTIR). The structures before and after heat treatment (90 °C, 1 &amp; 5 min) were investigated by Small-Angle X-ray Scattering (SAXS). SAXS intensities were evaluated using high-resolution models obtained as predictions from the AlphaFold Protein Structure Database. Interfacial and foaming properties were also evaluated. Findings: Both PA1 and PA2 contained various isoforms, and PA2 displayed a high β-sheet/α-helix ratio. In solution, SAXS intensities of PA1 could be predicted by its native structure, and after heating PA1 showed limited aggregation. PA2 could be presented as a dimer, which unfolded and formed large aggregates during heating. The high-resolution models could also explain well the SAXS signal of the unfractionated PA, combining PA1 and PA2. After heating, PA2 dominated the properties of the PA mixtures. PA2 predominantly contributed to the interfacial and foaming properties of PA, in spite of both PA1 and PA2 showing adsorption at the air/water interface. Indeed, PA1 in isolation could not form a stable foam. Perspective: SAXS data analyzed with high-resolution structure models allowed for an in depth understanding of the structural changes of PA1 and PA2, and provided a mechanistic understanding of the relationships between structure, composition, and technological functionality of the albumin fractions from pea.</p>}},
  author       = {{Li, Ruifen and Neofytos, Dionysios and Kirkensgaard, Jacob J.K. and Pal, Antara and Pedersen, Jan Skov and Corredig, Milena}},
  issn         = {{0021-9797}},
  keywords     = {{Foaming; Heat-induced aggregates; Interfacial properties; PA1; PA2; Pea albumins; SAXS; Secondary structure}},
  language     = {{eng}},
  publisher    = {{Academic Press}},
  series       = {{Journal of Colloid and Interface Science}},
  title        = {{In-depth exploration of the structure of pea albumin, its fractions and their heating and foaming properties}},
  url          = {{http://dx.doi.org/10.1016/j.jcis.2025.137507}},
  doi          = {{10.1016/j.jcis.2025.137507}},
  volume       = {{692}},
  year         = {{2025}},
}