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Figure 6 | Biotechnology for Biofuels

Figure 6

From: Ligninolytic peroxidase genes in the oyster mushroom genome: heterologous expression, molecular structure, catalytic and stability properties, and lignin-degrading ability

Figure 6

Demonstration of lignin-degrading ability of P. ostreatus VP. (A) Oxidative degradation of a nonphenolic lignin model dimer by VP1. The erythro (dotted line) and threo (dashed line) isomers of 14C-labeled 4-ethoxy-3-methoxyphenylglycerol-β-guaiacyl ether (peak 1) were treated with VP1, and the completed reactions were analyzed by HPLC. The main products were 4-ethoxy-3-methoxybenzaldehyde (peak 2) and 1-(4-ethoxy-3-methoxyphenyl)-3-hydroxy-2-(2-methoxyphenoxy)-propan-1-one (peak 3). The minor peaks 4 and 5 correspond to 1-(4-ethoxy-3-methoxyphenyl)-2,3-dihydroxypropan-1-one and 1-(4-ethoxy-3-methoxyphenyl)glycerol, respectively. (B, C) Lignin depolymerization by VP1.14C-labeled synthetic lignin (DHP) was treated with VP1 from the P. ostreatus genome in the presence (B) and absence (C) of VA. Black symbols indicate reactions with enzyme and open symbols indicate controls without enzyme. Total recoveries of initially added 14C from complete reactions before GPC analysis were 62% for reaction B and 92% for reaction C. Recoveries from control reactions were somewhat higher as reported earlier [22]. The arrows indicate elution volumes of two polystyrene molecular mass standards (1,800 and 500 Da) and VA (168 Da). DHP, dehydrogenation polymer; GPC, gel permeation chromatography; HPLC, high performance liquid chromatography; VA, veratryl alcohol; VP, versatile peroxidase.

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