The J-aggregation of rneso-tetra (4-sulfonatophenyl) porphine (TPPS4) on a plant-esterase-functionalized surface in a 1:1 v/v mixture of 0.05 M HCl/ethanol (pH similar to 1.38) was analyzed in real time using a quartz crystal microbalance with dissipation monitoring (QCM-D). Simultaneous changes in frequency (Delta f) and energy dissipation (Delta D) correlated well with mass and structural changes during the sequential phases of slow nucleation, rapid aggregation, and equilibration in J-aggregation. The time-dependent mass adsorption could be quantitatively analyzed with a model, which integrated two simple equations obtained when the surface concentration of TPPS4 (Gamma(TPPS4)) was below and above the critical aggregation surface concentration (CASC). This study provides a new view for the protein-induced J-aggregation process, which may be helpful for understanding the interactions of self-assembled nanostructures with biomolecules.