Bovine serum albumin also enhances catechol browning with impacts to its electrophoretic mobility BSA enhanced catechol browning following similar trends similar to simple amines, but showed distinct concentration-and pH-dependent effects (Fig. ). In unbuffered assays, browning rates increased to ~6x baseline, peaking at ~22-24 mg/mL BSA before slightly declining at higher concentrations (Fig. ). Starting pH measurements revealed a progressive increase with BSA concentration: 7.50 at 2 mg/mL, 8.02 at 12 mg/mL, and 8.11 at 32 mg/mL (Table ), suggesting that BSA functions as both an effective protein buffer and a nucleophile capable of reacting with catechol. In Pi-buffered assays, browning rates exhibited more pronounced bell-shaped relationships. At pH 7.4, browning rates peaked between ~14-16 mg/mL BSA, reaching ~5x baseline before declining rapidly. Measured pH remained stable (7.95-7.94) across this range. At pH 7.8, peak rates occurred at ~20-24 mg/mL BSA, achieving ~9x baseline rates followed by a decline despite stable pH ). These trends, including the decline in browning rates at higher BSA concentrations despite stable or rising pH, warrant further investigation.