FN Archimer Export Format
PT J
TI Characterization of New Oligosaccharides Obtained by An Enzymatic Cleavage of the Exopolysaccharide Produced by the Deep-Sea Bacterium Alteromonas infernus Using its Cell Extract
BT 
AF AKOUMANY, Katy
   ZYKWINSKA, Agata
   SINQUIN, Corinne
   MARCHAND, Laetitia
   Fanuel, Mathieu
   Ropartz, David
   Rogniaux, Hélène
   Pipelier, Muriel
   DELBARRE LADRAT, Christine
   COLLIEC JOUAULT, Sylvia
AS 1:1,2;2:1;3:1;4:1;5:3;6:3;7:3;8:2;9:1;10:1;
FF 1:PDG-RBE-BRM-LEMMMB;2:PDG-RBE-BRM-LEMMMB;3:PDG-RBE-BRM-LEMMMB;4:PDG-RBE-BRM-LEMMMB;5:;6:;7:;8:;9:PDG-RBE-BRM-LEMMMB;10:PDG-RBE-BRM-LEMMMB;
C1 Ifremer, Laboratoire Ecosystèmes Microbiens et Molécules Marines pour les Biotechnologies, F-44311 Nantes, France
   Université de Nantes, CNRS, Chimie et Interdisciplinarité: Synthèse, Analyse, Modélisation (CEISAM), UMR CNRS 6230, Faculté des Sciences et des Techniques, F-44322 Nantes, France
   INRA, UR1268 Biopolymères Interactions Assemblages, F-44300 Nantes, France;
C2 IFREMER, FRANCE
   UNIV NANTES, FRANCE
   INRA, FRANCE
SI NANTES
SE PDG-RBE-BRM-LEMMMB
IN WOS Ifremer UPR
   DOAJ
   copubli-france
   copubli-p187
   copubli-univ-france
IF 0.182
TC 9
UR https://archimer.ifremer.fr/doc/00515/62644/67021.pdf
LA English
DT Article
DE ;deep-sea bacterium;Alteromonas infernus;wild-type strain;exopolysaccharides;glycosaminoglycan-mimetic;enzymatic depolymerization;structural analysis;mass spectrometry
AB 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. 
PY 2019
PD OCT
SO Molecules
SN 1420-3049
PU MDPI AG
VL 24
IS 19
UT 000496242300026
DI 10.3390/molecules24193441
ID 62644
ER

EF