Hofmeister anion effects synergize with microbial transglutaminase to enhance the techno-functional properties of pea protein

Pea protein are emerging as the most potential alternative for meat products, but its application was hindered by their weaker gelling properties. Here, the feasibility of combining the Hofmeister anion (CO32-, Citrate3-, and SO42-) effect with microbial transglutaminase (MTG) cross-linking strategy to improve the techno-functional properties of pea protein was studied. Hofmeister anions or/and MTG treatment of pea protein caused a clear shift in far-UV CD spectra towards beta-turn and random coil structures. Furthermore, Hofmeister anion and MTG-induced crosslinking caused a reduction of surface hydrophobicity in contrast with anions-treated. Compared to CO32- and SO42-, Citrate3-treatment can better improve the efficiency of MTG-crosslinking, as demonstrated by a reduction in free amino group contents and an increase in mean diameter size. Using MTG in combination with Hofmeister anions showed significantly improved foam property and gel hardness as well as decrease gelation temperature of pea protein, specifically Citrate3-treatment. Thus, this research provides a novel and effective method to improve the effect of MTG-cross-linked pea protein, which will play an essential role in future food production.