Characterization of a GH17 laminarinase, <i>Ml</i> GH17A, from a laminarin polysaccharide utilization locus in the marine bacterium <i>Muricauda lutaonensis</i>

species and is suggested to play a crucial role in the utilization of laminarin by these bacteria. IMPORTANCE: GH17A possessed more glycone subsites (-1 to -4), attributed to the β3-α3 loop, which was longer than in GH17 plant β-glucanases.

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Publication Details

Journal
Applied and Environmental Microbiology
Published
2026-04-06
DOI
https://doi.org/10.1128/aem.00141-26
Primary Topic
Polysaccharides and Plant Cell Walls
Type
article
Field-Weighted Citation Impact
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article

Characterization of a GH17 laminarinase, Ml GH17A, from a laminarin polysaccharide utilization locus in the marine bacterium Muricauda lutaonensis

Antoine Moenaert, Zehui Dong, Eva Nordberg Karlsson, Ólafur H. Friðjónsson et al.
Applied and Environmental Microbiology
Polysaccharides and Plant Cell Walls
article

Characterization of a GH17 laminarinase, Ml GH17A, from a laminarin polysaccharide utilization locus in the marine bacterium Muricauda lutaonensis

Antoine Moenaert, Zehui Dong, Eva Nordberg Karlsson, Ólafur H. Friðjónsson, Justyna M. Dobruchowska, Maik G N Derks, Javier A. Linares-Pastén, Guðmundur Óli Hreggviðsson, Leila Allahgholi
article en

Abstract

species and is suggested to play a crucial role in the utilization of laminarin by these bacteria. IMPORTANCE: GH17A possessed more glycone subsites (-1 to -4), attributed to the β3-α3 loop, which was longer than in GH17 plant β-glucanases.

Applied and Environmental Microbiology
Lund University (SE), Utrecht University (NL), Institute for Biomedicine (IT), Pharmo Institute (NL)
Life below water
Openalex Percentile: Top 26%
Polysaccharides and Plant Cell Walls
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