Myofibrillar protein (MP)-soluble aggregates can be made by tactics of gallic acid (GA) modification during pH shifting, and this work aimed to disclose their aggregation pattern and in vitro digestion behavior. GA modification dissociated the filamentous structure of myofibrils and caused structural reassembly to form small-sized aggregates. These aggregates were evidenced to contain GA-bridged dimers and oligomers of myosin or actin, having a molecular weight of ∼1225 kDa. Additionally, the structural rearrangement significantly decreased the surface hydrophobicity while substantially increased the surface charge. As a result, the obtained colloidal solution was translucent and heat-resistant. Intriguingly, MP-soluble aggregates exhibited a retarded digestive behavior. Further evaluation by a quartz crystal microbalance suggested that the reduced binding affinity of soluble aggregates toward gastric pepsin could be the underlying reason. This work may foster the engineering advances of modulating the MP structure-digestion for the tailor manufacturing of muscle protein-based beverages.