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<p>Pea, faba bean, and soy protein isolates (PPI, FPI, SPI) are increasingly used as primary ingredients for developing plant-based gels for cheese and meat analogues. A major challenge is their limited functionality, including low solubility, poor emulsifying capacity, and restricted molecular flexibility, which together constrain their ability to form strong and cohesive gels. Controlled protein modification and optimized processing conditions are therefore required to tailor their gelation behaviour. This study aimed to modify the gelation properties of PPI, FPI, and SPI using protein glutaminase (PG) and transglutaminase (TG), and to evaluate fermentation-induced gelation in emulsion-based systems relevant for future plant-based food applications. PG treatment resulted in 12–16% deamidation across the three proteins but increased solubility only in SPI, while zeta potential remained unchanged, indicating minimal changes in net surface charge. Lactic-acid bacteria fermentation enhanced gelation for all proteins, yielding gel hardness values of 46–102&#xa0;g and confirming that acidification is the primary driver of network formation. TG addition during fermentation markedly increased gel hardness in all proteins (128–402&#xa0;g), with the strongest effect observed in SPI. PG treatment alone did not affect the hardness of fermented gels, but it modulated TG-induced gelation in a protein-specific manner. In SPI, PG reduced TG-induced gel hardness to 303&#xa0;g, likely due to increased soluble proteins and water retention, whereas FPI showed no change and PPI exhibited a slight increase to 176&#xa0;g. These findings highlight the interplay between PG-induced deamidation and TG-mediated cross-linking and demonstrate that these interactions are strongly protein dependent.</p>

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Comparative Effects of Protein Glutaminase and Transglutaminase on Fermentation-Induced Gelation of Pea, Faba Bean, and Soy Protein Isolates

  • 期刊论文

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  • 发表日期：

    2026年8月1日

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  • Ashwitha Poojary,
  • Ourania Gouseti,
  • Poul Erik Jensen

摘要

Pea, faba bean, and soy protein isolates (PPI, FPI, SPI) are increasingly used as primary ingredients for developing plant-based gels for cheese and meat analogues. A major challenge is their limited functionality, including low solubility, poor emulsifying capacity, and restricted molecular flexibility, which together constrain their ability to form strong and cohesive gels. Controlled protein modification and optimized processing conditions are therefore required to tailor their gelation behaviour. This study aimed to modify the gelation properties of PPI, FPI, and SPI using protein glutaminase (PG) and transglutaminase (TG), and to evaluate fermentation-induced gelation in emulsion-based systems relevant for future plant-based food applications. PG treatment resulted in 12–16% deamidation across the three proteins but increased solubility only in SPI, while zeta potential remained unchanged, indicating minimal changes in net surface charge. Lactic-acid bacteria fermentation enhanced gelation for all proteins, yielding gel hardness values of 46–102 g and confirming that acidification is the primary driver of network formation. TG addition during fermentation markedly increased gel hardness in all proteins (128–402 g), with the strongest effect observed in SPI. PG treatment alone did not affect the hardness of fermented gels, but it modulated TG-induced gelation in a protein-specific manner. In SPI, PG reduced TG-induced gel hardness to 303 g, likely due to increased soluble proteins and water retention, whereas FPI showed no change and PPI exhibited a slight increase to 176 g. These findings highlight the interplay between PG-induced deamidation and TG-mediated cross-linking and demonstrate that these interactions are strongly protein dependent.