Perspectives for biocatalytic lignin utilization: cleaving 4-O-5 and C-alpha-C-beta bonds in dimeric lignin model compounds catalyzed by a promiscuous activity of tyrosinase

Title
Perspectives for biocatalytic lignin utilization: cleaving 4-O-5 and C-alpha-C-beta bonds in dimeric lignin model compounds catalyzed by a promiscuous activity of tyrosinase
Authors
엄영순김연제민경선염태우김지예우한민상병인유영제김용환
Keywords
lignin; tyrosinase; Sustainable lignin utilization; Promiscuous activity; 4-Phenoxyphenol; Guaiacyl glycerol-β-guaiacyl ether (GGE)
Issue Date
2017-09
Publisher
BIOTECHNOLOGY FOR BIOFUELS
Citation
VOL 10-212-8
Abstract
Background: 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. Results: 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. Conclusion: 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.
URI
http://pubs.kist.re.kr/handle/201004/66647
ISSN
1754-6834
Appears in Collections:
KIST Publication > Article
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