Depolymerization of biorefinery lignin by improved laccases of the white-rot fungus Obba rivulosa

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Wallenius , J , Kontro , J , Lyra , C , Kuuskeri , J , Wan , X , Kahkonen , M A , Baig , I , Kamer , P C J , Sipila , J , Makela , M R , Nousiainen , P & Hilden , K 2021 , ' Depolymerization of biorefinery lignin by improved laccases of the white-rot fungus Obba rivulosa ' , Microbial Biotechnology , vol. 14 , no. 5 , pp. 2140-2151 . https://doi.org/10.1111/1751-7915.13896

Title: Depolymerization of biorefinery lignin by improved laccases of the white-rot fungus Obba rivulosa
Author: Wallenius, Janne; Kontro, Jussi; Lyra, Christina; Kuuskeri, Jaana; Wan, Xing; Kahkonen, Mika A.; Baig, Irshad; Kamer, Paul C. J.; Sipila, Jussi; Makela, Miia R.; Nousiainen, Paula; Hilden, Kristiina
Other contributor: University of Helsinki, Department of Microbiology
University of Helsinki, Department of Chemistry
University of Helsinki, Fungal Genetics and Biotechnology
University of Helsinki, Fungal Genetics and Biotechnology
University of Helsinki, Department of Microbiology
University of Helsinki, Department of Microbiology
University of Helsinki, Department of Chemistry
University of Helsinki, Helsinki Institute of Sustainability Science (HELSUS)
University of Helsinki, Department of Chemistry
University of Helsinki, Fungal Genetics and Biotechnology





Date: 2021-09
Language: eng
Number of pages: 12
Belongs to series: Microbial Biotechnology
ISSN: 1751-7915
DOI: https://doi.org/10.1111/1751-7915.13896
URI: http://hdl.handle.net/10138/334678
Abstract: Fungal laccases are attracting enzymes for sustainable valorization of biorefinery lignins. To improve the lignin oxidation capacity of two previously characterized laccase isoenzymes from the white-rot fungus Obba rivulosa, we mutated their substrate-binding site at T1. As a result, the pH optimum of the recombinantly produced laccase variant rOrLcc2-D206N shifted by three units towards neutral pH. O. rivulosa laccase variants with redox mediators oxidized both the dimeric lignin model compound and biorefinery poplar lignin. Significant structural changes, such as selective benzylic alpha-oxidation, were detected by nuclear magnetic resonance analysis, although no polymerization of lignin was observed by gel permeation chromatography. This suggests that especially rOrLcc2-D206N is a promising candidate for lignin-related applications.
Subject: 116 Chemical sciences
BOND-CLEAVAGE
OXIDATION
LIGNOCELLULOSE
PEROXIDASE
MEDIATORS
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