Jain S, et al. Food Chemistry, 2024, 449, 139179.
Propylene glycol alginate (PGA) binds to pea proteins via transacylation to enhance pea protein function. The transacylation reaction was conducted at a pH of 11.0, with varying mass ratios of pea protein isolate (PPI) to PGA and different reaction times, in a sonic bath maintained at 40 °C. The optimal degree of glycation was observed at a 45-minute reaction time, with mass ratios of 2:1 (37.73%) and 1:1 (35.96%). Ultrasonication significantly enhanced glycation, as confirmed by gel electrophoresis. The glycation process increased the random coil content of pea proteins by 28%, leading to improvements in their solubility (2.02 times higher at pH 7.0), water-holding capacity (over 50% at pH 7.0), foaming properties, emulsifying properties, and heat stability.
To prepare the PGA-pea protein conjugates, PGA was dissolved in deionized water and stirred overnight, while PPI dispersions were prepared in sodium phosphate buffer at different pH levels (10.0, 11.0, 12.0). The PPI mixtures were treated in an ultrasonic water bath, where the temperature was meticulously maintained at 40 °C. Post-reaction, the pH was neutralized to 7.0, and the mixture was centrifuged to obtain a supernatant, which was then lyophilized.
This study demonstrates that conjugating pea proteins with PGA via transacylation, enhanced by ultrasonication, significantly improves their functional properties, making them more suitable for various food and beverage applications.