Transglutaminase modifies the stability and digestibility of chickpea- protein-stabilized oil-in-water emulsions

Chickpea is an abundantly grown legume with high protein content considered as a good source of protein concentrates for food applications. This study sought to utilize enzymatic crosslinking to modulate the properties of chickpea-stabilized o/w emulsions. A stable 40% o/w emulsion was obtained with 6% (w/w) of chickpea protein followed by crosslinking with transglutaminase (TG). Crosslinking with TG increased emulsion stability, poly-dispersity and particle size and led to the formation of a gel-like structure (G`>G″). Microscopy visualization demonstrated the formation of an aggregated and dense emulsion droplets network. In vitro digestion of TG-crosslinked chickpea-stabilized emulsions were characterized with a different protein pattern and decreased digestibility than the non-crosslinked digesta. Proteomic analyses imply that crosslinked chickpea emulsion is source of bioactive peptides that are liberated by human digestive enzymes. The results demonstrate that enzymatic crosslinking of chickpea protein is a useful approach for tailoring novel plant based food matrices with potentially controlled energy intake.