Abstract
There is a need to better understand the possible anti-nutritional effect of food stabilizers on the digestibility of important macronutrients, like proteins. This study hypothesized that the anionic nature of κ-, ι-, λ-, Carrageenan (CGN) and xanthan gum directs their interactions with food proteins leading to their subsequent attenuated digestive proteolysis. Model chocolate milk drinks were tested for their colloidal properties, viscosity and proteolytic breakdown in adults and children using in vitro digestion models coupled with proteomic analyses. SDS-PAGE analyses of gastro-intestinal effluents highlight stabilizers hinder protein breakdown in adults and children. Zeta potential and colloidal particle size were the strongest determinants of stabilizers' ability to hinder proteolysis. LC-MS proteomic analyses revealed stabilizer addition significantly reduced bioaccessibility of milk-derived bioactive peptides with differences in liberated peptide sequences arising mainly from their location on the outer rim of the protein structures. Further, liberation of bioactive peptides emptying from a child stomach into the intestine were most affected by the presence of ι-CGN. Overall, this study raises the notion that stabilizer charge and other properties of edible proteins are detrimental to the ability of humans to utilize the nutritional potential of such formulations. This could help food professionals and regulatory agencies carefully consider the use of anionic stabilizers in products aiming to serve as protein sources for children and other liable populations.