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Peer-reviewedCC BYFood Chemistry

Production of mung bean protein isolates by isoelectric precipitation and ultrafiltration-diafiltration: impact on the composition, structural and techno-functional properties as well as in vitro digestibility

Abstract

The techno-functional properties of plant-based protein ingredients are critical for developing food formulations and greatly depend on the production method. The physicochemical and techno-functional properties, as well as the in vitro digestibility, of mung bean protein isolates (MBPIs) produced by isoelectric precipitation (IEP) and ultrafiltration-diafiltration (UFDF) were compared. Both MBPIs had comparable protein contents (~84%) but the protein structure was slightly affected by isolation method, as MBPI-IEP exhibited lower surface hydrophobicity and slightly higher denaturation temperature. These differences were likely due to albumin proteins in MBPI-UFDF, absent in MBPI-IEP. Additionally, the MBPI-UFDF exhibited lower foam stability but higher gel firmness. Protein and peptide profiles after in vitro oral and gastric digestion were similar. Overall, proteolysis during intestinal digestion was more pronounced in MBPI-IEP. These findings highlight the importance of selecting the MBPI production process based on the desired food formulations, despite its low impact on in vitro digestibility. • MBPI production method had little effect on overall composition. • Albumin presence in MBPI-UFDF might influenced protein structure and functionality. • Proteolysis during intestinal digestion was more pronounced in MBPI-IEP than in MBPI-UFDF.

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BibTeX
@article{duboislaurin2026production,
  title = {{Production of mung bean protein isolates by isoelectric precipitation and ultrafiltration-diafiltration: impact on the composition, structural and techno-functional properties as well as in vitro digestibility}},
  author = {Florence Dubois-Laurin and Ugo Berthelot and Alexia Gravel and Véronique Perreault and Haïrati Aboubacar and Barbara Deracinois and Christophe Flahaut and Rozenn Ravallec and Benoit Cudennec and Guillaume Brisson and Alain Doyen},
  journal = {Food Chemistry},
  year = {2026},
  month = nov,
  doi = {10.1016/j.foodchem.2026.149560},
  url = {https://hal.science/hal-05847691v1},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Production of mung bean protein isolates by isoelectric precipitation and ultrafiltration-diafiltration: impact on the composition, structural and techno-functional properties as well as in vitro digestibility
AU  - Florence Dubois-Laurin
AU  - Ugo Berthelot
AU  - Alexia Gravel
AU  - Véronique Perreault
AU  - Haïrati Aboubacar
AU  - Barbara Deracinois
AU  - Christophe Flahaut
AU  - Rozenn Ravallec
AU  - Benoit Cudennec
AU  - Guillaume Brisson
AU  - Alain Doyen
PY  - 2026
DA  - 2026/11/02
JO  - Food Chemistry
DO  - 10.1016/j.foodchem.2026.149560
UR  - https://hal.science/hal-05847691v1
AB  - The techno-functional properties of plant-based protein ingredients are critical for developing food formulations and greatly depend on the production method. The physicochemical and techno-functional properties, as well as the in vitro digestibility, of mung bean protein isolates (MBPIs) produced by isoelectric precipitation (IEP) and ultrafiltration-diafiltration (UFDF) were compared. Both MBPIs had comparable protein contents (~84%) but the protein structure was slightly affected by isolation method, as MBPI-IEP exhibited lower surface hydrophobicity and slightly higher denaturation temperature. These differences were likely due to albumin proteins in MBPI-UFDF, absent in MBPI-IEP. Additionally, the MBPI-UFDF exhibited lower foam stability but higher gel firmness. Protein and peptide profiles after in vitro oral and gastric digestion were similar. Overall, proteolysis during intestinal digestion was more pronounced in MBPI-IEP. These findings highlight the importance of selecting the MBPI production process based on the desired food formulations, despite its low impact on in vitro digestibility. • MBPI production method had little effect on overall composition. • Albumin presence in MBPI-UFDF might influenced protein structure and functionality. • Proteolysis during intestinal digestion was more pronounced in MBPI-IEP than in MBPI-UFDF.
SN  - 0308-8146
SN  - 1873-7072
ER  -