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Enzyme Microb Technol. 2014 Nov;66:74-9. doi: 10.1016/j.enzmictec.2014.08.011. Epub 2014 Sep 3.

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

Author information

1
Department of Chemical Engineering, Kwangwoon University, 447-1, Wolgye-Dong, Nowon-Gu, Seoul 139-701, Republic of Korea.
2
Department of Chemical Engineering, Kwangwoon University, 447-1, Wolgye-Dong, Nowon-Gu, Seoul 139-701, Republic of Korea. Electronic address: metalkim@kw.ac.kr.

Abstract

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:

Free-hydroxyl phenolic group; Lignin peroxidase; Lignin-degradation; O-Methyltransferase

PMID:
25248703
DOI:
10.1016/j.enzmictec.2014.08.011
[Indexed for MEDLINE]

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