Enzymes specific for the κ and λ fractions of carrageenan were obtained from the cell-free culture medium of Pseudomonas carrageenovora. These enzymes were concentrated by precipitation with ammonium sulfate and separated by chromatography on hydroxylapatite.The κ-carrageenase was purified to electrophoretic homogeneity by incubation at 35 °C and chromatography on DEAE cellulose. The enzymic hydrolysis of κ-carrageenan was accompanied by a rapid fall in specific viscosity and increase in reducing power. The products were a homologous series of sulfated oligosaccharides with 3-O-(3,6-anhydro-α-D-galactopyranosyl)-D-galactopyranose-4-O-sulfate (neocarrabiose-4-O-sulfate) as the major degradation product, and an enzyme-resistant fraction. The alkali-modified enzyme-resistant fraction was degraded by the κ-carrageenase.
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Weigl et al. (1966) studied this question.
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