Notably, the deconvoluted C1s spectra (Figure ) showed the difference in prominent bonds, C-C (sp2), C-O/C-N, and C=O. The BNNS-Arg@Lac spectra exhibited peak area ratios of 28:20:15 for C-C, C-O/C-N, and C=O respectively, aligning with the typical bond ratios found in laccase's chemical architecture. Given the XPS surface detection limit and larger molecule size, laccase should represent the primary composition detected if it covered the surface. The peak emergence concurs with the anticipated bond chemistry inherent to the enzyme's structure. range of pH levels and temperatures. As illustrated in Figure , both laccases showed optimal performance at a pH of 3. However, at conditions approaching a neutral pH, BNNS-Arg@Lac retained more activity, whereas natural laccase nearly lost all its activity when the pH was adjusted to 5.5. Given that most environmentally relevant reactions occur around 15 °C, the stability of enzymatic catalysts at these mild temperatures is crucial. We assessed the performance of the two laccase forms across a temperature range of 20 °C to 70 °C (Figure ).