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Provedor de dados:  ArchiMer
País:  France
Título:  Characterization of New Oligosaccharides Obtained by An Enzymatic Cleavage of the Exopolysaccharide Produced by the Deep-Sea Bacterium Alteromonas infernus Using its Cell Extract
Autores:  Akoumany, Katy
Zykwinska, Agata
Sinquin, Corinne
Marchand, Laetitia
Fanuel, Mathieu
Ropartz, David
Rogniaux, Hélène
Pipelier, Muriel
Delbarre Ladrat, Christine
Colliec Jouault, Sylvia
Data:  2019-10
Ano:  2019
Palavras-chave:  Deep-sea bacterium
Alteromonas infernus
Wild-type strain
Exopolysaccharides
Glycosaminoglycan-mimetic
Enzymatic depolymerization
Structural analysis
Mass spectrometry
Resumo:  Bacteria from deep-sea hydrothermal vents constitute an attractive source of bioactive molecules. In particular, exopolysaccharides (EPS) produced by these bacteria become a renewable source of both biocompatible and biodegradable molecules. The low molecular weight (LMW) derivatives of the GY785 EPS produced by the deep-sea hydrothermal vent strain Alteromonas infernus have previously displayed some biological properties, similar to those of glycosaminoglycans (GAG), explored in cancer and tissue engineering. These GAG-mimetic derivatives are obtained through a free radical depolymerization process, which could, however, affect their structural integrity. In a previous study, we have shown that A. infernus produces depolymerizing enzymes active on its own EPS. In the present study, an enzymatic reaction was optimized to generate LMW derivatives of the GY785 EPS, which could advantageously replace the present bioactive derivatives obtained by a chemical process. Analysis by mass spectrometry of the oligosaccharide fractions released after enzymatic treatment revealed that mainly a lyase activity was responsible for the polysaccharide depolymerization. The repeating unit of the GY785 EPS produced by enzyme cleavage was then fully characterized.
Tipo:  Text
Idioma:  Inglês
Identificador:  https://archimer.ifremer.fr/doc/00515/62644/67021.pdf

DOI:10.3390/molecules24193441

https://archimer.ifremer.fr/doc/00515/62644/
Editor:  MDPI AG
Formato:  application/pdf
Fonte:  Molecules (1420-3049) (MDPI AG), 2019-10 , Vol. 24 , N. 19 , P. 3441 (15p.)
Direitos:  info:eu-repo/semantics/openAccess

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