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Involvement of laccase-like enzymes in humic substance degradation by diverse polar soil bacteria

Cited 3 time in wos
Cited 3 time in scopus

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dc.contributor.authorPark, Ha Ju-
dc.contributor.authorLee, Yung Mi-
dc.contributor.authorDo, Hackwon-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorKim, Eungbin-
dc.contributor.authorLee, Hyoungseok-
dc.contributor.authorKim, Dockyu-
dc.date.accessioned2022-07-07T04:46:59Z-
dc.date.available2022-07-07T04:46:59Z-
dc.date.issued2021-01-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/13583-
dc.description.abstractHumic substances (HS) in soil are widely distributed in cold environments and account for a significant fraction of soil's organic carbon. Bacterial strains (n = 281) were isolated at 15 degrees C using medium containing humic acids (HA), a principal component of HS, from a variety of polar soil samples: 217 from the Antarctic and 64 from the Arctic. We identified 73 potential HA-degrading bacteria based on 16S rRNA sequence similarity, and these sequences were affiliated with phyla Proteobacteria (73.9%), Actinobacteria (20.5%), and Bacteroidetes (5.5%). HA-degrading strains were further classified into the genera Pseudomonas (51 strains), Rhodococcus (10 strains), or others (12 strains). Most strains degraded HA between 10 and 25 degrees C, but not above 30 degrees C, indicating cold-adapted degradation. Thirty unique laccase-like multicopper oxidase (LMCO) gene fragments were PCR-amplified from 71% of the 73 HA-degrading bacterial strains, all of which included conserved copper-binding regions (CBR) I and II, both essential for laccase activity. Bacterial LMCO sequences differed from known fungal laccases; for example, a cysteine residue between CBR I and CBR II in fungal laccases was not detected in bacterial LMCOs. This suggests a bacterial biomarker role for LMCO to predict changes in HS-degradation rates in tundra regions as global climate changes. Computer-aided molecular modeling showed these LMCOs contain a highly-conserved copper-dependent active site formed by three histidine residues between CBR I and CBR II. Phylogenetic- and modeling-based methods confirmed the wide occurrence of LMCO genes in HA-degrading polar soil bacteria and linked their putative gene functions with initial HS-degradation processes.en_US
dc.languageEnglishen_US
dc.language.isoenen_US
dc.subjectBiotechnology & Applied Microbiologyen_US
dc.subjectMicrobiologyen_US
dc.subject.classificationKing Sejong Stationen_US
dc.titleInvolvement of laccase-like enzymes in humic substance degradation by diverse polar soil bacteriaen_US
dc.title.alternative극지토양 미생물에 의한 부식질 분해과정에서 Laccase 효소의 역할 규명en_US
dc.typeArticleen_US
dc.identifier.bibliographicCitationPark, Ha Ju, et al. 2021. "Involvement of laccase-like enzymes in humic substance degradation by diverse polar soil bacteria". <em>FOLIA MICROBIOLOGICA</em>, 66(3): 331-340.-
dc.citation.titleFOLIA MICROBIOLOGICAen_US
dc.citation.volume66en_US
dc.citation.number3en_US
dc.identifier.doi10.1007/s12223-020-00847-9-
dc.citation.startPage331en_US
dc.citation.endPage340en_US
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2019:78.205en_US
dc.subject.keywordBiodegradationen_US
dc.subject.keywordCold-adapteden_US
dc.subject.keywordHumic acidsen_US
dc.subject.keywordLaccaseen_US
dc.subject.keywordPolaren_US
dc.subject.keywordSoil bacteriaen_US
dc.identifier.localId2021-0024-
dc.identifier.scopusid2-s2.0-85100080919-
dc.identifier.wosid000609060500003-
Appears in Collections  
2020-2020, Ecophysiology of KGI terrestrial organisms to reveal mechanisms of adaptation to changing environment (20-20) / Lee, Hyoungseok (PE20170)
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