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CAZyme analysis and functional characterization of a new GH18 chitin hydrolase from Gelidibacter salicanalis PAMC21136

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Title
CAZyme analysis and functional characterization of a new GH18 chitin hydrolase from Gelidibacter salicanalis PAMC21136
Other Titles
남극 토양미생물 (Gelidibacter salicanalis PAMC21136) 에서 유래한 새로운 GH18 키틴 가수분해효소의 CAZyme 분석 및 기능적 특성 규명
Authors
Lakshan Paudel
Bashu Dev Pardhe
So-Ra Han
Lee, Jun Hyuck
Tae-Jin Oh
Keywords
Antarctic bacteriaCAZymeChitooligomersExo-chitinaseGH18N-acetyl D-glucosamine
Issue Date
2025-03
Citation
Lakshan Paudel, et al. 2025. "CAZyme analysis and functional characterization of a new GH18 chitin hydrolase from Gelidibacter salicanalis PAMC21136". Carbohydrate Polymer Technologies and Applications, 10(0): 100773-0.
Abstract
Gelidibacter salicanalis strains remain poorly understood in terms of their genomic attributes and are rarely reported for the degradation of polysaccharides within the niche. Gelidibacter salicanalis PAMC21136, an Antarctic isolate, was sequenced and functionally annotated. 251 genes were classified into the CAZyme families, which includes the highest number of GH family, highlighting peculiarity towards various macro biopolymers. Further, based on domain architecture and multiple sequence alignment, gene belonging to the family18 glycoside hydrolase was identified as chitinase. The gene encoding chitinase (MBJ7879808.1) was successfully cloned and expressed in Escherichia coli BL21 cells. MBJ7879808.1 demonstrated activity towards colloidal chitin but there was no detectable activity towards microcrystalline crab shell chitin. Enzyme exhibited an exo-pattern of hydrolysis on both colloidal chitin, and shorter chain GlcNAc oligomers namely [(GlcNAc)3, (GlcNAc)4, (GlcNAc)5, and (GlcNAc)6] producing GlcNAc as a single final product. Biochemical characterization revealed an optimum activity at 25 °C and pH 7.0. Mn²? ions significantly enhanced the activity by 1.7-fold. Turnover number (Kcat) was 8.6 min?1 and catalytic efficiency (Kcat/Km) was 2.0ml/mg/min towards the substrate colloidal chitin. These findings expanded the polysaccharide degradation capability of Gelidibacter salicanalis PAMC21136 and highlight the biotechnological potential of the GH18 enzyme towards production of chitooligomers.
URI
https://repository.kopri.re.kr/handle/201206/16586
DOI
http://dx.doi.org/10.1016/j.carpta.2025.100773
Type
Article
Station
King Sejong Station
Indexed
국외기타
Appears in Collections  
2025-2025, 미생물-식물 유전체와 대사체 기반 생리활성물질 개발 및 식물 회복력 시스템 구축 (25-25) / 이준혁 (PN25170)
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