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Kim, Yong Hwan
Enzyme and Protein Engineering Lab.
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dc.citation.endPage 220 -
dc.citation.startPage 212 -
dc.citation.volume 10 - Min, Kyoungseon - Yum, Taewoo - Kim, Jiye - Woo, Han Min - Kim, Yunje - Sang, Byoung‑In - Yoo, Young Je - Kim, Yong Hwan - Um, Youngsoon - 2023-12-21T21:46:34Z - 2023-12-21T21:46:34Z - 2017-09-13 - 2017-09 -
dc.description.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.
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.
dc.identifier.bibliographicCitation BIOTECHNOLOGY FOR BIOFUELS, v.10, pp.212 - 220 -
dc.identifier.doi 10.1186/s13068-017-0900-3 -
dc.identifier.issn 1754-6834 -
dc.identifier.scopusid 2-s2.0-85029177922 -
dc.identifier.uri -
dc.identifier.url -
dc.identifier.wosid 000410042600001 -
dc.language 영어 -
dc.publisher BIOMED CENTRAL LTD -
dc.title 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 -
dc.type Article -
dc.description.isOpenAccess TRUE -
dc.relation.journalWebOfScienceCategory Biotechnology & Applied Microbiology; Energy & Fuels -
dc.relation.journalResearchArea Biotechnology & Applied Microbiology; Energy & Fuels -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordAuthor Sustainable lignin utilization -
dc.subject.keywordAuthor Tyrosinase -
dc.subject.keywordAuthor Promiscuous activity -
dc.subject.keywordAuthor 4-Phenoxyphenol -
dc.subject.keywordAuthor Guaiacyl glycerol-beta-guaiacyl ether (GGE) -
dc.subject.keywordPlus SITE-DIRECTED MUTAGENESIS -
dc.subject.keywordPlus RHODOCOCCUS-JOSTII RHA1 -
dc.subject.keywordPlus AGARICUS-BISPORUS -
dc.subject.keywordPlus L-DOPA -
dc.subject.keywordPlus PEROXIDASE -
dc.subject.keywordPlus OXIDATION -
dc.subject.keywordPlus ENZYMES -
dc.subject.keywordPlus DEGRADATION -
dc.subject.keywordPlus SPECIFICITY -
dc.subject.keywordPlus PATHWAYS -


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