Fig. 3

Cleavage of 4-O-5 bond in 4-phenoxyphenol by the catalytic promiscuity of tyrosinase. a GC profile and mass spectra (MS) of the catalytic product using 4-phenoxyphenol in the absence (control, blue line) and presence of 100 unit tyrosinase (reactant, red line). The analyte was extracted with ethyl acetate. The chromatographic peaks were identified by the retention time and mass spectra library (NIST02). The authentic standard chemicals were used to confirm the identified (standard, black line). Inset: (i) mass spectrum and (ii) magnification of the peak at 10.15 min, and (iii) mass spectrum of the peak at 39.7 min. b Reaction scheme illustrates the catalytic promiscuity cleaves the 4-O-5 bond in 4-phenoxyphenol. The catalytic product phenol is a primary substrate of tyrosinase (cresolase activity)