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.
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July 1969
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Research Article|
July 01 1969
The specificity of an agarase from a Cytophaga species
M Duckworth;
M Duckworth
1Department of Chemistry, University College of North Wales, Bangor, Caerns
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J R Turvey
J R Turvey
1Department of Chemistry, University College of North Wales, Bangor, Caerns
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Publisher: Portland Press Ltd
© 1969 The Biochemical Society
1969
Biochem J (1969) 113 (4): 693–696.
Citation
M Duckworth, J R Turvey; The specificity of an agarase from a Cytophaga species. Biochem J 1 July 1969; 113 (4): 693–696. doi: https://doi.org/10.1042/bj1130693
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