TY - JOUR T1 - Characterization of New Oligosaccharides Obtained by An Enzymatic Cleavage of the Exopolysaccharide Produced by the Deep-Sea Bacterium Alteromonas infernus Using its Cell Extract A1 - Akoumany,Katy A1 - Zykwinska,Agata A1 - Sinquin,Corinne A1 - Marchand,Laetitia A1 - Fanuel,Mathieu A1 - Ropartz,David A1 - Rogniaux,Hélène A1 - Pipelier,Muriel A1 - Delbarre Ladrat,Christine A1 - Colliec Jouault,Sylvia AD - Ifremer, Laboratoire Ecosystèmes Microbiens et Molécules Marines pour les Biotechnologies, F-44311 Nantes, France AD - Université de Nantes, CNRS, Chimie et Interdisciplinarité: Synthèse, Analyse, Modélisation (CEISAM), UMR CNRS 6230, Faculté des Sciences et des Techniques, F-44322 Nantes, France AD - INRA, UR1268 Biopolymères Interactions Assemblages, F-44300 Nantes, France; UR - https://archimer.ifremer.fr/doc/00515/62644/ DO - 10.3390/molecules24193441 KW - deep-sea bacterium KW - Alteromonas infernus KW - wild-type strain KW - exopolysaccharides KW - glycosaminoglycan-mimetic KW - enzymatic depolymerization KW - structural analysis KW - mass spectrometry N2 - 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. Y1 - 2019/10 PB - MDPI AG JF - Molecules SN - 1420-3049 VL - 24 IS - 19 ID - 62644 ER -