Arabinoxylo- and Arabino-Oligosaccharides- Specific alpha-L-Arabinofuranosidase GH51 Isozymes from the Amylolytic Yeast Saccharomycopsis fibuligera
DC Field | Value | Language |
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dc.contributor.author | Park, Tae Hyeon | - |
dc.contributor.author | Choi, Chang-Yun | - |
dc.contributor.author | Kim, Hyeon Jin | - |
dc.contributor.author | Song, Jeong-Rok | - |
dc.contributor.author | Park, Damee | - |
dc.contributor.author | Kang, Hyun Ah | - |
dc.contributor.author | Kim, Tae-Jip | - |
dc.date.accessioned | 2021-08-10T03:40:07Z | - |
dc.date.available | 2021-08-10T03:40:07Z | - |
dc.date.issued | 2021-02 | - |
dc.identifier.issn | 1017-7825 | - |
dc.identifier.issn | 1738-8872 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/48042 | - |
dc.description.abstract | Two genes encoding probable alpha-L-arabinofuranosidase (E.C. 3.2.1.55) isozymes (ABFs) with 92.3% amino acid sequence identity, ABF51A and ABF51B, were found from chromosomes 3 and 5 of Saccharomycopsis fibuligera KJJ81, an amylolytic yeast isolated from Korean wheat-based nuruk, respectively. Each open reading frame consists of 1,551 nucleotides and encodes a protein of 517 amino acids with the molecular mass of approximately 59 kDa. These isozymes share approximately 49% amino acid sequence identity with eukaryotic ABFs from filamentous fungi. The corresponding genes were cloned, functionally expressed, and purified from Escherichia coli. SfABF51A and SfABF51B showed the highest activities on p-nitrophenyl arabinofuranoside at 40 similar to 45 degrees C and pH 7.0 in sodium phosphate buffer and at 50 degrees C and pH 6.0 in sodium acetate buffer, respectively. These exoacting enzymes belonging to the glycoside hydrolase (GH) family 51 could hydrolyze arabinoxylooligosaccharides (AXOS) and arabino-oligosaccharides (AOS) to produce only L-arabinose, whereas they could hardly degrade any polymeric substrates including arabinans and arabinoxylans. The detailed product analyses revealed that both SfABF51 isozymes can catalyze the versatile hydrolysis of alpha-(1,2)and alpha-(1,3)-L-arabinofuranosidic linkages of AXOS, and alpha-(1,2)-, alpha-(1,3)-, and alpha-(1,5)linkages of linear and branched AOS. On the contrary, they have much lower activity against the alpha(1,2) and alpha-(1,3)-double-substituted substrates than the single-substituted ones. These hydrolases could potentially play important roles in the degradation and utilization of hemicellulosic biomass by S. fibuligera. | - |
dc.format.extent | 8 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY | - |
dc.title | Arabinoxylo- and Arabino-Oligosaccharides- Specific alpha-L-Arabinofuranosidase GH51 Isozymes from the Amylolytic Yeast Saccharomycopsis fibuligera | - |
dc.type | Article | - |
dc.identifier.doi | 10.4014/jmb.2012.12038 | - |
dc.identifier.bibliographicCitation | JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.31, no.2, pp 233 - 240 | - |
dc.identifier.kciid | ART002690418 | - |
dc.description.isOpenAccess | Y | - |
dc.identifier.wosid | 000623844400008 | - |
dc.identifier.scopusid | 2-s2.0-85102537440 | - |
dc.citation.endPage | 240 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 233 | - |
dc.citation.title | JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY | - |
dc.citation.volume | 31 | - |
dc.type.docType | Article | - |
dc.publisher.location | 대한민국 | - |
dc.subject.keywordAuthor | Arabino-oligosaccharides | - |
dc.subject.keywordAuthor | Arabinoxylooligosaccharides | - |
dc.subject.keywordAuthor | L-arabinose | - |
dc.subject.keywordAuthor | Saccharomycopsis fibuligera | - |
dc.subject.keywordAuthor | α-L-arabinofuranosidases | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | GENE | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalResearchArea | Microbiology | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
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