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
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Do Young Kim | - |
| dc.contributor.author | Lee, Yung Mi | - |
| dc.contributor.author | Jong Suk Lee | - |
| dc.contributor.author | Hyangmi Kim | - |
| dc.contributor.author | Chung-Wook Chung | - |
| dc.date.accessioned | 2026-02-10T02:23:36Z | - |
| dc.date.available | 2026-02-10T02:23:36Z | - |
| dc.date.issued | 2025-10 | - |
| dc.identifier.uri | https://repository.kopri.re.kr/handle/201206/16580 | - |
| dc.description.abstract | Endo-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.language | English | en_US |
| dc.subject.classification | King Sejong Station | en_US |
| dc.title | 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 | en_US |
| dc.title.alternative | 남극 Glacieibacterium sp. PAMC 29367에서 유래한 새로운 저온 활성 GH8형 엔도-β-1,4-글루카나아제의 발견 및 특성 규명 | en_US |
| dc.type | Article | en_US |
| dc.identifier.bibliographicCitation | Do 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.title | Frontiers in Microbiology | en_US |
| dc.citation.volume | 16 | en_US |
| dc.citation.number | 0 | en_US |
| dc.identifier.doi | https://doi.org/10.3389/fmicb.2025.1682092 | - |
| dc.citation.startPage | 0 | en_US |
| dc.citation.endPage | 0 | en_US |
| dc.description.articleClassification | SCIE | - |
| dc.description.jcrRate | JCR 2023:0 | en_US |
| dc.subject.keyword | Antarctic | en_US |
| dc.subject.keyword | GH8 | en_US |
| dc.subject.keyword | Glacieibacterium sp. | en_US |
| dc.subject.keyword | broad pH stability | en_US |
| dc.subject.keyword | cold-adapted enzyme | en_US |
| dc.subject.keyword | endo-β-1 | en_US |
| dc.subject.keyword | 4-glucanase | en_US |
| dc.identifier.localId | 2025-0193 | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.