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Cited by 2Proteins in Food SystemsProtein Hydrolysis and Bioactive PeptidesProtein purification and stability

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Comparative impacts of physical and chemical modifications on pea protein concentrate: Effects on physicochemical properties

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Sharifi, Anahita, Ahmadi, Farhad, Ng, Ken, Maharjan, Pankaj, Walker, Cassandra, Suleria, Hafiz·2026·Food Research International
DOI 10.1016/j.foodres.2026.119198
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Abstract

Pea proteins are promising plant-based ingredients; however, their limited solubility restricts broader application. While pea protein isolates are widely studied, the modification of pea protein concentrate remains underexplored. This study compared four modification methods, two physical modifications (dry heating and ultrasonication), and two chemical modifications (pH shifting and Maillard conjugation with guar gum) to improve the solubility of pea protein concentrate. Optimal conditions were: dry heating (80 °C, 30 min), ultrasonication (70% amplitude, 5 min), pH shifting (pH 10, 3 h), and Maillard reaction (60 °C, 1 h). All treatments altered solubility, surface charge, hydrophobicity, particle size, and protein structure. Ultrasonication and pH shifting achieved the highest solubility improvements (96.4% and 92.62%, respectively, from an initial 73.1%). Maillard conjugation increased hydrophobicity but had a limited impact on solubility, with only a 6% increase, while dry heating showed the least change. Overall, all modifications increased the surface hydrophobicity of the proteins, while the proportions of α-helix and β-turn structures increased in all treatments except the conjugated protein. These findings indicate that each method affects pea protein concentrate differently, highlighting the importance of selecting techniques based on the intended application.

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  • Ultrasonication enhances both electrostatic and hydrophilic interactions in proteins, thereby enhancing protein hydrophilicity and solubility.

    “These findings suggest that ultrasonication enhances both electrostatic and hydrophilic interactions in proteins (Sharifi et al., 2026), thereby enhancing protein hydrophi­ licity and solubility (Zhu et al., 2025).”

    From Effects of ultrasonication on structure and gelation of plant proteins at different denaturation states (2027) · cites this paper as Sharifi et al., 2026

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Metadata

Authors
Sharifi, A., Ahmadi, F., Ng, K., Maharjan, P., Walker, C., & Suleria, H.
Affiliations
  • The University of Melbourne (AU)
  • Agriculture Victoria (AU)
Corresponding author
Suleria, Hafiz
ORCID
Venue
Food Research International
Publisher
Elsevier BV
Published
2026-07
Volume
235
Pages
119198
ISSN
0963-9969 (ISSN-L)
DOI
10.1016/j.foodres.2026.119198
OpenAlex
W7154527452
Cited by
2
References
0
Citations by year
2026: 2
FWCI
4.74
Type
journal article
Language
en
Open access
Licence
Locations
  • Food Research International (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Minerva Access (University of Melbourne) (submittedVersion, cc-by)
Funders
  • Agriculture Victoria
  • Australian Government Grains Research and Development Corporation (DEE2312-002RTX)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Protein Hydrolysis and Bioactive Peptides
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
Keywords
pea protein concentrate, protein solubility, physical modification, chemical modification, sonication, dry heating, pH change, Maillard reaction, guar gum, surface hydrophobicity, surface charge, protein secondary structure, plant proteins
MeSH terms
Pea Proteins, Food Handling, Hot Temperature, Hydrogen-Ion Concentration, Particle Size, Solubility, Maillard Reaction, Pisum sativum, Chemical Phenomena, Hydrophobic and Hydrophilic Interactions

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