Abstract
1. The extracellular agarase from a Cytophaga species was shown to have no action on neoagarobiose, neoagarotetraose or their analogues containing 6-O-methyl-d-galactose residues. 2. The action of the enzyme on neoagaro-octaose suggests that scission of the central β-d-galactosidic linkage, to form two molecules of tetrasaccharide, is the preferred mode of action; however, both exterior d-galactosidic linkages in the octasaccharide and both in neoagarohexaose are hydrolysed at a somewhat lower rate. 3. Sulphated oligosaccharides produced by prolonged enzyme action on porphyran have a minimum degree of polymerization of about 8–10units. 4. For such sulphated oligosaccharides to be further hydrolysed by enzyme action, it is suggested that an unmodified neoagarotetraose residue must be present in the oligosaccharide. 6. A new method for determining the degree of polymerization of these large oligosaccharides is described.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Duckworth M., Turvey J. R. An extracellular agarase from a Cytophaga species. Biochem J. 1969 Jun;113(1):139–142. doi: 10.1042/bj1130139. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Duckworth M., Turvey J. R. The action of a bacterial agarase on agarose, porphyran and alkali-treated porphyran. Biochem J. 1969 Jul;113(4):687–692. doi: 10.1042/bj1130687. [DOI] [PMC free article] [PubMed] [Google Scholar]