<Original>Lignin Peroxidase-Catalyzed Oxidation of Monomeric Lignin Model Substrates

Abstract

The substrate specificity of lignin peroxidase (LiP) was investigated by determining the K_ms and V_<max>s of LiP for the four lignin model substrates of 3,4-dimethoxybenzyl alcohol (I), 3,4-dimethoxybenzyl glycerol (II), 3,4,5-trimethoxybenzyl alcohol (III), and 3, 4, 5-trimethoxybenzyl glycerol (IV). The K_ms (μM) and V_<max>s (turnover number, sec^<-1>) of LiP were determined. The K_m/V_<max> values calculated to be 4.7, 18.2, 29.9, and 76.7 for I, II, III, and IV, respectively. Among the substrates tested, I (veratryl alcohol), which is a secondary metabolite of white-rot fungi, was found to be the best substrate for LiP.