Unknown

Dataset Information

0

Isolation and characterization of an endo-beta-galactosidase from Bacteroides fragilis.


ABSTRACT: Six strains of Bacteroides fragilis were examined and all found to produce endo-beta-galactosidase, an enzyme that hydrolyses internal beta-galactosidic linkages of oligosaccharides belonging to the poly-N-acetyl-lactosamine series, with the common structure GlcNAc beta 1 leads to 3Gal beta 1 leads to 4GlcNAc/Glc. The enzyme was produced without the addition of an inducer such as keratan sulphate. It was purified 7000-fold from the culture supernatant and obtained with a yield 4-10-fold greater than from sources described previously. The specificity of the enzyme towards bovine corneal keratan sulphate, milk oligosaccharides and the glycolipids lacto-N-neotetraosylceramide and lacto-N-tetraosylceramide closely resembled that of the endo-beta-galactosidase isolated from Escherichia freundii. A novel observation was that both enzymes hydrolysed the type 2 sequence, Gal beta 1 leads to 4GlcNAc beta 1 leads to 3Gal beta 1 leads to 4Glc, at about twice the rate of the type 1 isomer, Gal beta 1 leads to 3GlcNAc beta 1 leads to 3Gal beta 1 leads to 4Glc. Because of the ease of purification of the enzyme and high yield in the absence of contaminating glycosidases and proteinases, Bacteroides fragilis is a valuable source of endo-beta-galactosidase for the structural analysis of carbohydrate chains.

SUBMITTER: Scudder P 

PROVIDER: S-EPMC1152152 | biostudies-literature | 1983 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Isolation and characterization of an endo-beta-galactosidase from Bacteroides fragilis.

Scudder P P   Uemura K K   Dolby J J   Fukuda M N MN   Feizi T T  

The Biochemical journal 19830801 2


Six strains of Bacteroides fragilis were examined and all found to produce endo-beta-galactosidase, an enzyme that hydrolyses internal beta-galactosidic linkages of oligosaccharides belonging to the poly-N-acetyl-lactosamine series, with the common structure GlcNAc beta 1 leads to 3Gal beta 1 leads to 4GlcNAc/Glc. The enzyme was produced without the addition of an inducer such as keratan sulphate. It was purified 7000-fold from the culture supernatant and obtained with a yield 4-10-fold greater  ...[more]

Similar Datasets

| S-EPMC4899533 | biostudies-literature
| S-EPMC134936 | biostudies-literature
| S-EPMC5277507 | biostudies-literature
| S-EPMC108111 | biostudies-literature
2007-12-30 | GSE4583 | GEO
| S-EPMC107664 | biostudies-literature
| S-EPMC174377 | biostudies-other
| S-EPMC206660 | biostudies-other
| S-EPMC204626 | biostudies-other
| S-EPMC9692976 | biostudies-literature