Heat-induced unfolding facilitates plant protein digestibility during in vitro static infant digestion

Abstract

Soy protein is the main protein source for plant-based infant formula, whereas pea protein is considered as a potential alternative plant protein source. This study assessed the structural changes of soy and pea proteins after heating between 65 °C and 100 °C, and its effects on the in vitro digestibility in the context of infant digestion. We found that with increased heating intensity, both soy and pea proteins unfolded, manifested as the increased surface hydrophobicity, thereby potentially improving the accessibility to digestive enzymes. Their final in vitro digestibility increased from ∼ 30% of non-treated samples to ∼ 60% of 100 °C-heated samples for soy protein, and from ∼ 52% to ∼ 65% for pea protein. Surface hydrophobicity was strongly positively correlated to the overall digestibility. Therefore, the heating temperatures that enabled protein unfolding promoted the digestibility of soy and pea proteins under infant digestion conditions.