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Enzymatic production of sugar from fungi and fungi-infected lignocellulosic biomass by a new cellulosomal enzyme harboring N-acetyl-beta-D-glucosaminidase activity

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dc.contributor.authorLee, Myeong-Eun-
dc.contributor.authorShin, Sang Kyu-
dc.contributor.authorOh, Jeong-Joo-
dc.contributor.authorHwang, Dong-Hyeok-
dc.contributor.authorKo, Young Jin-
dc.contributor.authorHyeon, Jeong Eun-
dc.contributor.authorHan, Sung Ok-
dc.date.accessioned2021-08-30T05:03:36Z-
dc.date.available2021-08-30T05:03:36Z-
dc.date.created2021-06-18-
dc.date.issued2021-01-
dc.identifier.issn0960-8524-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/50613-
dc.description.abstractCellulosomes are scaffold proteins displaying enzymes on the cell wall to efficiently obtain nutrient sources. CcGlcNAcase is a novel cellulosomal component. Based on sequence analysis, CcGlcNAcase was predicted to be a chitinolytic enzyme based on high homology with the discoidin domain-containing protein and chitobiase/beta-hexosaminidase C terminal domain. CcGlcNAcase expression was notably increased when chitin was present. CcGlcNAcase produced N-acetyl-D-glucosamine from various lengths of N-acetyl-D-glucosamine. CcGlcNAcase bound to chitin (89%) and fungi (54.10%), whereas CcGlcNAcase exhibited a low binding ability to cellulose and xylan. CcGlcNAcase hydrolyzed fungi, yielding maximum 3.90 g/L N-acetyl-D-glucosamine. CcGlcNAcase enhanced cellulase toward fungi-infected lignocellulosic biomass, yielding 18 mg/L glucose (1.32-fold) and 1.72-fold increased total reducing sugar levels, whereas cellulase alone produced 13 mg/L glucose. Taken together, CcGlcNAcase can be utilized to enhance the degradation of fungi-infected lignocellulosic biomass and exhibits potential applications in the wood and sugar industry.-
dc.languageEnglish-
dc.language.isoen-
dc.publisherELSEVIER SCI LTD-
dc.subjectCHITIN-BINDING DOMAIN-
dc.subjectCLOSTRIDIUM-CELLULOVORANS-
dc.subjectANTIFUNGAL CHITINASE-
dc.subjectDEGRADATION-
dc.subjectENDOCHITINASE-
dc.subjectPURIFICATION-
dc.subjectEXPRESSION-
dc.titleEnzymatic production of sugar from fungi and fungi-infected lignocellulosic biomass by a new cellulosomal enzyme harboring N-acetyl-beta-D-glucosaminidase activity-
dc.typeArticle-
dc.contributor.affiliatedAuthorHan, Sung Ok-
dc.identifier.doi10.1016/j.biortech.2020.124242-
dc.identifier.scopusid2-s2.0-85092410723-
dc.identifier.wosid000613136600021-
dc.identifier.bibliographicCitationBIORESOURCE TECHNOLOGY, v.319-
dc.relation.isPartOfBIORESOURCE TECHNOLOGY-
dc.citation.titleBIORESOURCE TECHNOLOGY-
dc.citation.volume319-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaAgriculture-
dc.relation.journalResearchAreaBiotechnology & Applied Microbiology-
dc.relation.journalResearchAreaEnergy & Fuels-
dc.relation.journalWebOfScienceCategoryAgricultural Engineering-
dc.relation.journalWebOfScienceCategoryBiotechnology & Applied Microbiology-
dc.relation.journalWebOfScienceCategoryEnergy & Fuels-
dc.subject.keywordPlusCHITIN-BINDING DOMAIN-
dc.subject.keywordPlusCLOSTRIDIUM-CELLULOVORANS-
dc.subject.keywordPlusANTIFUNGAL CHITINASE-
dc.subject.keywordPlusDEGRADATION-
dc.subject.keywordPlusENDOCHITINASE-
dc.subject.keywordPlusPURIFICATION-
dc.subject.keywordPlusEXPRESSION-
dc.subject.keywordAuthorN-acetyl-beta-D-glucosaminidase-
dc.subject.keywordAuthorChitin-
dc.subject.keywordAuthorFungi degradation-
dc.subject.keywordAuthorCellulosome-
dc.subject.keywordAuthorClostridium cellulovorans-
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