Low colloidal stability of myofibrillar protein (MP) during heating is a technofunctional constraint encountered in its beverage application. Gallic acid (GA), a natural polyphenol, was applied to fabricate MP soluble aggregates for an enhanced thermal stability. Upon pH shifting, GA was grafted into MP with the cysteine and tryptophan residues being the binding sites. As a result, the antioxidant activity of MP was enhanced. Additionally, GA modification decreased the α-helix structure of MP and converted MP into cross-linked aggregates. At low dosages (10 and 25 μmol/g GA), disulfide-dominant covalent bonds were formed to generate myosin and actin aggregates, while MP aggregates were mostly bridged through GA-thiols or GA-tryptophan adducts when the dosages exceeded 50 μmol/g. Such aggregates prevented MP from thermal gelation, leading to a stable and tunable colloidal state. This work can foster technological advances in the tailor manufacture of muscle protein-based beverages for special dietary uses.