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Identification and characterization of a novel, low-temperature-active GH8 endo-β-1,4-glucanase exhibiting broad pH stability from Antarctic Glacieibacterium sp. PAMC 29367

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dc.contributor.authorDo Young Kim-
dc.contributor.authorLee, Yung Mi-
dc.contributor.authorJong Suk Lee-
dc.contributor.authorHyangmi Kim-
dc.contributor.authorChung-Wook Chung-
dc.date.accessioned2026-02-10T02:23:36Z-
dc.date.available2026-02-10T02:23:36Z-
dc.date.issued2025-10-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/16580-
dc.description.abstractEndo-β-1,4-glucanase plays an essential role in the breakdown of cellulosic substances that consist of D-glucose units linked by β-1,4-glycosidic bonds. In this work, the gene encoding a novel extracellular glycoside hydrolase (GH) family 8 endo-β-1,4-glucanase (GluS) from Glacieibacterium sp. PAMC 29367, an Antarctic lichen (Megaspora verrucosa)-associated bacterial species, was identified, cloned, and characterized. The GluS gene (1080-bp) was predicted to express a non-modular endo-β-1,4-glucanase (38,347 Da) that possesses a single catalytic GH8 domain, showing 65.5% amino acid sequence identity with an uncharacterized endoglucanase from Alphaproteobacteria bacterium (GenBank accession number: PZN92894). Recombinant endo-β-1,4-glucanase proteins (rGluS: 39.0 kDa) produced in Escherichia coli BL21 exhibited the highest carboxymethylcellulose (CMC)-degrading activity at pH 5.0 and 40°C, while maintaining over 80% of maximal endo-β-1,4-glucanase activity even at 25°C. Furthermore, the enzyme exhibited notable stability across a broad pH range from 4.5 to 10.0. rGluS activity was greatly stimulated by >1.3-fold in the presence of 1 mM Co2+, whereas it was nearly completely inhibited by 0.5% sodium dodecyl sulfate or 5 mM N-bromosuccinimide. The specific activity (31.1 U mg?1) and kcat/Km (11.02 mg?1 s?1 mL) values of rGluS for CMC were marginally greater than those for barley β-1,3-1,4-glucan, with a specific activity of 28.9 U mg?1 and kcat/Km of 8.79 mg?1 s?1 mL for barley β-1,3-1,4-glucan. The recombinant enzyme demonstrated no detectable biocatalytic activity for p-nitrophenylglucopyranoside, p-nitrophenylcellobioside, D-cellobiose, and D-cellotriose, while it could cleave D-cellotetraose to generate two molecules of D-cellobiose. Moreover, rGluS-mediated degradation of D-cellopentaose led mainly to D-cellobiose production along with D-glucose and D-cellotriose, while its hydrolysis of CMC yielded D-cellotriose as the dominant end product, accompanied by D-glucose, D-cellobiose and D-cellotetraose. The substrate preferences and degradation profiles of rGluS on cellulosic materials supported its classification as a true GH8 endo-acting β-1,4-glucanase without transglycosylation activity. The findings of this study suggest that rGluS represents a novel, highly active, cold-adapted GH8 endo-β-1,4-glucanase exhibiting broad pH stability, and may serve as an effective candidate for low-temperature processing in the food and textile industries.en_US
dc.languageEnglishen_US
dc.subject.classificationKing Sejong Stationen_US
dc.titleIdentification and characterization of a novel, low-temperature-active GH8 endo-β-1,4-glucanase exhibiting broad pH stability from Antarctic Glacieibacterium sp. PAMC 29367en_US
dc.title.alternative남극 Glacieibacterium sp. PAMC 29367에서 유래한 새로운 저온 활성 GH8형 엔도-β-1,4-글루카나아제의 발견 및 특성 규명en_US
dc.typeArticleen_US
dc.identifier.bibliographicCitationDo Young Kim, et al. 2025. "Identification and characterization of a novel, low-temperature-active GH8 endo-β-1,4-glucanase exhibiting broad pH stability from Antarctic Glacieibacterium sp. PAMC 29367". <em>Frontiers in Microbiology</em>, 16(0): 0-0.-
dc.citation.titleFrontiers in Microbiologyen_US
dc.citation.volume16en_US
dc.citation.number0en_US
dc.identifier.doihttps://doi.org/10.3389/fmicb.2025.1682092-
dc.citation.startPage0en_US
dc.citation.endPage0en_US
dc.description.articleClassificationSCIE-
dc.description.jcrRateJCR 2023:0en_US
dc.subject.keywordAntarcticen_US
dc.subject.keywordGH8en_US
dc.subject.keywordGlacieibacterium sp.en_US
dc.subject.keywordbroad pH stabilityen_US
dc.subject.keywordcold-adapted enzymeen_US
dc.subject.keywordendo-β-1en_US
dc.subject.keyword4-glucanaseen_US
dc.identifier.localId2025-0193-
Appears in Collections  
2025-2025, 환경변화에 따른 남극 육상생물의 생리생태 반응 규명 (25-25) / 이형석 (PE25130)
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