1. A purified extracellular agarase from a Cytophaga species was used to hydrolyse agarose, porphyran and alkali-treated porphyran. 2. The hydrolysate from agarose was separated by gel filtration into the series of neoagarosaccharides, the predominant member of which was the tetrasaccharide. 3. Enzyme action on alkali-treated porphyran gave neoagarosaccharides and other oligosaccharides containing 6-O-methyl-d-galactose units. From the composition of these oligosaccharides it is deduced that action of the enzyme on a d-galactosidic linkage is four to five times faster than on the 6-O-methyl-d-galactosidic linkage. 4. Enzyme action on native porphyran gives a similar series of oligosaccharides but in smaller yield, much of the polysaccharide being either not degraded or only degraded to a series of large, highly sulphated oligosaccharides. 5. For porphyran, it is concluded that 6-O-methyl ether groups are distributed randomly on half the d-galactose units, but that the 6-sulphate groups on l-galactose units tend to occur in blocks.
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July 1969
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Research Article|
July 01 1969
The action of a bacterial agarase on agarose, porphyran and alkali -treated porphyran
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): 687–692.
Citation
M Duckworth, J R Turvey; The action of a bacterial agarase on agarose, porphyran and alkali -treated porphyran. Biochem J 1 July 1969; 113 (4): 687–692. doi: https://doi.org/10.1042/bj1130687
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