期刊
GLYCOBIOLOGY
卷 32, 期 4, 页码 276-288出版社
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwab125
关键词
brown algae; GH107; mass spectrometry; Pelvetia canaliculata; sulfated fucans
资金
- French National Research Agency
The extracellular matrix of brown algae is a rich source of fucose-containing sulfated polysaccharides (FCSPs). In this study, researchers used an enzyme called MfFcnA to deconstruct the structure of sulfated fucans from Pelvetia canaliculata, a type of brown algae. They found that the structure of these sulfated fucans is more complex than initially expected, with diverse species and branching structures. This study highlights the potential for MfFcnA to produce structurally diverse oligofucan products that could be screened for bioactivities.
The extracellular matrix of brown algae represents an abundant source of fucose-containing sulfated polysaccharides (FCSPs). FCSPs include sulfated fucans, essentially composed of fucose, and highly heterogeneous fucoidans, comprising various monosaccharides. Despite a range of potentially valuable biological activities, the structures of FCSPs are only partially characterized and enzymatic tools leading to their deconstruction are rare. Previously, the enzyme MfFcnA was isolated from the marine bacterium Mariniflexile fucanivorans and biochemically characterized as an endo-alpha-1 -> 4-l-fucanase, the first member of glycoside hydrolase family 107. Here, MfFcnA was used as an enzymatic tool to deconstruct the structure of the sulfated fucans from Pelvetia canaliculata (Fucales brown alga). Oligofucans released by MfFcnA at different time points were characterized using mass spectrometry coupled with liquid chromatography and tandem mass spectrometry through Charge Transfer Dissociation. This approach highlights a large diversity in the structures released. In particular, the analyses show the presence of species with less than three sulfates per two fucose residues. They also reveal species with monosaccharides other than fucose and the occurrence of laterally branched residues. Precisely, the lateral branching is either in the form of a hexose accompanied by a trisulfated fucose nearby, or of a side chain of fucoses with a pentose as the branching point on the polymer. Overall, the results indicate that the structure of sulfated fucans from P. canaliculata is more complex than expected. They also reveal the interesting capacity of MfFcnA to accommodate different substrates, leading to structurally diverse oligofucan products that potentially could be screened for bioactivities.
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