Human gastrointestinal conditions affect in vitro digestibility of peanut and bread proteins.

As plant proteins are increasingly used as a source of amino acids in the diet, studies on in vitro digestion of plant proteins are key to understand the different factors affecting proteolysis, with the ultimate goal of optimising the nutritional composition/intake of plant protein-rich products. More realistic scenarios including the most likely food matrix and physiologically relevant gastrointestinal (GI) conditions should be considered when assessing the in vitro digestion of proteins. The research described here compares the extent of hydrolysis of proteins from peanuts and wheat bread, in particular the vicilin-like 7S globulin (Ara h 1) and gliadin, respectively, with three GI scenarios simulating either infant, early phase adult (fed state) or late phase adult (fasted state) conditions. The digestibility of these proteins, in isolation or when naturally present in the respective food matrix, has been evaluated with SDS-PAGE, LC-MS/MS and a spectrophotometric assay. Results from the food matrices showed lower extent of total protein GI digestion under simulated infant conditions, intermediate behaviour under fed state adult conditions and larger extent under fasted state adult conditions. This was also the case for isolated gliadin. However, isolated Ara h 1 only showed lower extent of proteolysis in the gastric phase under infant conditions, reaching a similar extent to both adult conditions over the course of the intestinal phase. The food matrix seems to have delayed the proteolysis. Choosing an appropriate GI scenario as well as the matrix of the end food product is paramount when assessing in vitro protein digestion.