TY - JOUR
T1 - Depolymerization of biorefinery lignin by improved laccases of the white-rot fungus Obba rivulosa
AU - Wallenius, Janne
AU - Kontro, Jussi
AU - Lyra, Christina
AU - Kuuskeri, Jaana
AU - Wan, Xing
AU - Kähkönen, Mika A.
AU - Baig, Irshad
AU - Kamer, Paul C.J.
AU - Sipilä, Jussi
AU - Mäkelä, Miia R.
AU - Nousiainen, Paula
AU - Hildén, Kristiina
N1 - Funding Information:
This research was supported by the European Commission Horizon 2020 project FALCON, grant no: 720918 (JW, CL, JKo, MK, PN, XW, JS and KH), Marie Curie ITN network SuBiCat FP7, grant no: 607044 (IB, PK and KH) and the Academy of Finland grants no: 297847 (JKo and JKu) and no: 308284 (MRM). The authors wish to acknowledge CSC – IT Center for Science, Finland, for computational resources. MSc. Susanne Fritsche and BSc. Milla Koponen are thanked of their skillful technical assistance.
Funding Information:
This research was supported by the European Commission Horizon 2020 project FALCON, grant no: 720918 (JW, CL, JKo, MK, PN, XW, JS and KH), Marie Curie ITN network SuBiCat FP7, grant no: 607044 (IB, PK and KH) and the Academy of Finland grants no: 297847 (JKo and JKu) and no: 308284 (MRM).
Publisher Copyright:
© 2021 The Authors. Microbial Biotechnology published by Society for Applied Microbiology and John Wiley & Sons Ltd.
PY - 2021/9
Y1 - 2021/9
N2 - 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 α-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.
AB - 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 α-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.
UR - http://www.scopus.com/inward/record.url?scp=85111632742&partnerID=8YFLogxK
U2 - 10.1111/1751-7915.13896
DO - 10.1111/1751-7915.13896
M3 - Article
AN - SCOPUS:85111632742
SN - 1751-7915
VL - 14
SP - 2140
EP - 2151
JO - Microbial Biotechnology
JF - Microbial Biotechnology
IS - 5
ER -