Enhancing the functionality of pea proteins by conjugation with propylene glycol alginate via transacylation reaction assisted with ultrasonication

Pea proteins lack the desirable functional characteristics for food and beverage applications. In this study, transacylation reaction assisted with ultrasonication was used to glycate pea proteins with propylene glycol alginate to enhance their functional properties. The reaction was carried out at pH 11.0 for different pea protein isolate: propylene glycol alginate mass ratios and time durations in a sonic bath at 40 °C. Glycation was confirmed in gel electrophoresis, and ultrasonication enhanced the glycation, with optimal degrees of glycation observed at 45 min reaction time and mass ratios of 2:1 (37.73%) and 1:1 (35.96%). The transacylation reaction increased random coil content of pea proteins by 28% and enhanced their solubility by 2.02 times at pH 7.0, water holding capacity by >50% at pH 7.0, foaming properties, emulsifying properties, and heat stability. This study offers a novel approach that can enhance functionality and applicability of pea proteins. •Pea protein-alginate conjugates were prepared using the transacylation reaction.•Ultrasonication was used during the reaction to increase the degree of glycation.•Protein: polysaccharide mass ratios of 2:1 and 1:1 and 45 min led to optimal glycation.•Conjugation increased the random coil content and decreased the rigidity of proteins.•Conjugation significantly improved the functionality of pea protein isolate.