Bacteria belonging to the Burkholderia cepacia complex (Bcc) are interesting for their involvement in pulmonary infections in patients affected by cystic fibrosis (CF) or chronic granulomatous disease. Many Bcc strains isolated from CF patients produce high amts. of exopolysaccharides (EPS). Although different strains sometimes biosynthesize different EPS, the majority of Bcc bacteria produce only one type of polysaccharide, which is called cepacian. The polymer has a unique heptasaccharidic repeating unit, contg. three side chains, and up to three O-acetyl substituents. We here report for the first time the isolation and characterization of a lyase active towards cepacian produced by a Bacillus sp., which was isolated in our lab. The enzyme mol. mass, evaluated by size-exclusion chromatog., is 32,700±1500 Da. The enzyme catalyzes a ß-elimination reaction of the disaccharide side chain ß-D-Galp-(1?2)-a-D-Rhap-1? from the C-4 of the glucuronic acid residue present in the polymer backbone. Although active on both native and de-acetylated cepacian, the enzyme showed higher activity on the latter polymer.
First report of a lyase for cepacian, the polysaccharide produced by Burkholderia cepacia complex bacteria
G Impallomeni;
2006
Abstract
Bacteria belonging to the Burkholderia cepacia complex (Bcc) are interesting for their involvement in pulmonary infections in patients affected by cystic fibrosis (CF) or chronic granulomatous disease. Many Bcc strains isolated from CF patients produce high amts. of exopolysaccharides (EPS). Although different strains sometimes biosynthesize different EPS, the majority of Bcc bacteria produce only one type of polysaccharide, which is called cepacian. The polymer has a unique heptasaccharidic repeating unit, contg. three side chains, and up to three O-acetyl substituents. We here report for the first time the isolation and characterization of a lyase active towards cepacian produced by a Bacillus sp., which was isolated in our lab. The enzyme mol. mass, evaluated by size-exclusion chromatog., is 32,700±1500 Da. The enzyme catalyzes a ß-elimination reaction of the disaccharide side chain ß-D-Galp-(1?2)-a-D-Rhap-1? from the C-4 of the glucuronic acid residue present in the polymer backbone. Although active on both native and de-acetylated cepacian, the enzyme showed higher activity on the latter polymer.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.