Inducing the structural interplay of binary pulse protein complex to stimulate the solubilization of chickpea (Cicer arietinum L.) protein isolate.

ABSTRACT

Chickpea protein (CP) is an exceptional nutrient-dense pulse protein prevailing in the development of plant-based foods. However, its relatively low solubility, compared to other legume proteins, hinders the practical uses of CP in food matrix. To resolve this problem, pea protein (PP), another popular pulse protein, was co-assembled with CP to form a binary complex during the alkaline pH-shifting process. Results indicated that the complexed CP exhibited significantly increased solubility to that of the pristine protein (more than 50%), whose aqueous stability was also enhanced against different environmental stresses (pH, salt, heat/frozen treatment, and centrifugation). Structural and morphology analysis confirmed the interplay between unfolded CP and PP during pH shifting, which enabled their resistance to acid-induced structural over-folding. Our experiments that induce the co-assembling of two pulse proteins provide a novel routine and scientific basis for tailoring CP functionalities, as well as the formulation of pulse protein-based products.