This study aimed to investigate how food structure, in the form of different ovalbumin aggregate morphologies, impacted the proteolysis of ovalbumin using an in vitro model that simulated digestion in the adult gastrointes- tinal tract. Four different aggregate morphologies were prepared by heating ovalbumin solution using different combinations of pH and ionic strength. Quantitative peptidomics (label-free) and multivariate data analysis of the resulting in vitro digests were performed. The 593 identified peptides were distributed in 6 homogeneous clusters based on the relative amount of peptide release from the different aggregate morphologies. Each cluster gatheredpeptideswithcommonphysicochemicalcharacteristics.Theresultssuggestthatpepticandchymotryp- tic cleavages were favored by aggregation regardless of the aggregate morphology, while tryptic cleavages were favored when ovalbumin aggregates were spherical-agglomerated. It is notable that even after extensive diges- tion, the initial aggregate morphology in fluenced the amount of each peptide released