S-Space College of Engineering/Engineering Practice School (공과대학/대학원) Dept. of Chemical and Biological Engineering (화학생물공학부) Journal Papers (저널논문_화학생물공학부)
Perspectives for biocatalytic lignin utilization: cleaving 4-O-5 and Cα–Cβ bonds in dimeric lignin model compounds catalyzed by a promiscuous activity of tyrosinase
- Min, Kyoungseon; Yum, Taewoo; Kim, Jiye; Woo, Han Min; Kim, Yunje; Sang, Byoung-In; Yoo, Young Je; Kim, Yong Hwan; Um, Youngsoon
- Issue Date
- BioMed Central
- Biotechnology for Biofuels, 10(1):212
- Sustainable lignin utilization; Tyrosinase; Promiscuous activity; 4-Phenoxyphenol; Guaiacyl glycerol-βguaiacyl ether; GGE
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In the biorefinery utilizing lignocellulosic biomasses, lignin decomposition to value-added phenolic derivatives is a key issue, and recently biocatalytic delignification is emerging owing to its superior selectivity, low energy consumption, and unparalleled sustainability. However, besides heme-containing peroxidases and laccases, information about lignolytic biocatalysts is still limited till date.
Herein, we report a promiscuous activity of tyrosinase which is closely associated with delignification requiring high redox potentials (>1.4 V vs. normal hydrogen electrode [NHE]). The promiscuous activity of tyrosinase not only oxidizes veratryl alcohol, a commonly used nonphenolic substrate for assaying ligninolytic activity, to veratraldehyde but also cleaves the 4-O-5 and Cα–Cβ bonds in 4-phenoxyphenol and guaiacyl glycerol-β-guaiacyl ether (GGE) that are dimeric lignin model compounds. Cyclic voltammograms additionally verified that the promiscuous activity oxidizes lignin-related high redox potential substrates.
These results might be applicable for extending the versatility of tyrosinase toward biocatalytic delignification as well as suggesting a new perspective for sustainable lignin utilization. Furthermore, the results provide insight for exploring the previously unknown promiscuous activities of biocatalysts much more diverse than ever thought before, thereby innovatively expanding the applicable area of biocatalysis.