Graphical AbstractSummary:Bench-top and pilot-scale experiments were conducted to produce an enriched phospholipid (PL) fraction from whey protein phospholipid concentrate (WPPC). Five different protease enzymes were used individually for the enzymatic hydrolysis of proteins in a rehydrated WPPC solution (5% wt/vol). Alcalase exhibited the most proteolytic activity as determined using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profiles and was therefore chosen for the pilot-scale experiment. Alcalase enzyme hydrolyzed most of the large protein aggregates (20-150 μm) present in the WPPC solution into smaller protein aggregates (0.3-20 μm) and small peptides helping the release of some of the fat and PL from the protein aggregates. Microfiltration (polyvinylidene fluoride membrane with 0.1-μm pore size) along with diafiltration was used to remove peptides from the hydrolyzed protein solution via the permeate and to concentrate the PL and fat to produce a partially enriched PL concentrate with 9.3% PL (dry basis) in the final product.