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Fig. 2 | Biotechnology for Biofuels

Fig. 2

From: Experimental and theoretical insights into the effects of pH on catalysis of bond-cleavage by the lignin peroxidase isozyme H8 from Phanerochaete chrysosporium

Fig. 2

Product distribution from bond cleavage of fluorous-tagged GGE by wildtype lignin peroxidase (a) and acid-stabilized mutant of the same peroxidase (b). The reaction contained 1 mM of NIMS-tagged phenolic lignin dimer, 5 µM of LiPH8 enzyme, 20 mM of veratryl alcohol as mediator was performed in sodium acetate buffer pH 2. 6–5.0. The reaction was started by adding H2O2 fed at a rate of 250 uM every 30 min up to 3 h. Error bars are the standard deviation for three replicates, and the first column at each pH condition in Fig. 1 is the mean and standard deviation of the products from both β-O-4′ ether and Cα-C1 bond cleavage combined. The means and standard deviations for β-O-4′ bond cleavage were 65.5 ± 0.8 (pH 2.6), 60.0 ± 1.3 (pH 3.0), 38.4 ± 1.0 (pH 4.0) and 26.5 ± 0.4 (pH 5.0). The means and standard deviations for Cα-C1 bond cleavage were 27.0 ± 4.3 (pH 2.6), 26.24 ± 4.5 (pH 3.0), 13.0 ± 5.0 (pH 4.0 and 11.9 ± 3.0 (pH 5.0)

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