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Accelerated degradation of lignin by lignin peroxidase isozyme H8 (LiPH8) from Phanerochaete chrysosporium with engineered 4-O-methyltransferase from Clarkia breweri

Paper ID Volume ID Publish Year Pages File Format Full-Text
16995 42629 2014 6 PDF Available
Title
Accelerated degradation of lignin by lignin peroxidase isozyme H8 (LiPH8) from Phanerochaete chrysosporium with engineered 4-O-methyltransferase from Clarkia breweri
Abstract

•4-OH phenolics were methylated by methyltransferase from Clarkia breweri.•Inhibition of phenolics toward LiP was eliminated through methylation.•Veratryl alcohol was intensively oxidized by co-use of methyltransferase and LiP.

Free-hydroxyl phenolic units can decrease or even abort the catalytic activity of lignin peroxidase H8 during oxidation of veratryl alcohol and model lignin dimers, resulting in slow and inefficient lignin degradation. In this study we applied engineered 4-O-methyltransferase from Clarkia breweri to detoxify the inhibiting free-hydroxyl phenolic groups by converting them to methylated phenolic groups. The multistep, enzyme-catalyzed process that combines 4-O-methyltransferase and lignin peroxidase H8 suggested in this work can increase the efficiency of lignin-degradation. This study also suggests approaching the field of multi-enzyme in vitro systems to improve the understanding and development of plant biomass in biorefinery operations.

Keywords
Lignin peroxidase; O-Methyltransferase; Free-hydroxyl phenolic group; Lignin-degradation
First Page Preview
Accelerated degradation of lignin by lignin peroxidase isozyme H8 (LiPH8) from Phanerochaete chrysosporium with engineered 4-O-methyltransferase from Clarkia breweri
Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 66, November 2014, Pages 74–79
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering