Proteins secreted by, or displayed on the surface tegument of, trematodes have key functions in the host-parasite interaction. As such, they are often leading targets for diagnostic tests or vaccine candidates. Here we describe methods for the isolation and analysis of soluble secreted proteins (i.e., the secretome) released during in vitro culture of adult Fasciola hepatica. We also describe two methods for the enrichment of proteins displayed on the outer tegumental surface of F. hepatica. These approaches enable downstream identification of the isolated proteins by mass spectrometry-based proteomics.