The raising consumer demand for plant-derived proteins has led to an increased production of alternative protein ingredients with varying processing histories. In this study, we used a commercially available potato protein ingredient with a nutritionally valuable amino acid profile and high technological functionality to evaluate if the digestibility of a suspension with the same composition is affected by differences in the structure. Four isocaloric (4% protein, w/w) matrices (suspension, gel, foam and heat-set foam) were prepared and their gastrointestinal fate was followed utilizing a semi-dynamic in vitro digestion model. The microstructure was observed by confocal laser scanning microscopy, protein breakdown was tested by electrophoresis and free amino acids after intestinal digestion was estimated using liquid chromatography/triple-quadruple-mass spectrometry (LC-TQMS). The heat-treated samples showed a higher degree of hydrolysis and lower trypsin inhibitory activity than the non-heat-treated samples. An in vitro digestible indispensable amino acid score was calculated based on experimental data, showing a value of 0.9 based on sulfur amino acids/valine as the limiting amino acids. The heated samples also showed a slower gastric emptying rate. The study highlights the effect of the food matrix on the distribution of the peptides created during various stages of gastric emptying.
- amino acid digestibility
- potato protein isolate
- semi-dynamic in vitro digestion