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A highly efficient chitosanase producer, the actinomycete N174, identified by chemotaxonomic methods as belonging to the genus Streptomyces was isolated from soil. Chitosanase production by N174 was inducible by chitosan or D-glucosamine. In culture filtrates the chitosanase accounted for 50-60% of total extracellular proteins. The chitosanase was purified by polyacrylic acid precipitation, CM-Sepharose and gel permeation chromatography. The maximum velocity of chitosan degradation was obtained at 65 ° C when the pH was maintained at 5.5. The enzyme degraded chitosans with a range of acetylation degrees from 1 to 60% but not chitin or CM-cellulose. The enzyme showed an endo-splitting type of activity and the end-product of chitosan degradation contained a mixture of dimers and trimers of D-glucosamine.

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A method for the preparation of hydrogels from the complexation of chitosan and xanthan is reported. Stable hydrogels capable of retaining be tween 65 and 95% weight water were prepared. The water retention and prop erties of the hydrogels were studied as a function of the degree of acetylation of chitosan and the ratio chitosan/xanthan used in the preparation of the gel. Spectroscopic FTIR was used to confirm complexation between the amine (chi tosan) and carboxylic (xanthan) groups. Electron micrographs (SEM and TEM) show the formation of a fibrillar structure with characteristic pore sizes be tween 100 and 1000 nm and fibril diameters between 50 and 100 nm. The diffu sion coefficient of 4- O-methyl- d-glucurono-D-xylan Remazol Brilliant Blue R (RBB-xylan) in the complex chitosan-xanthan was 2.02 × 10-12 m 2s-1 at 30°C. The chitosan-xanthan complex was used to immobilize two enzymes (endo-1,4- β-xylanase and protease) either as single enzymes or as a binary system. Immo bilization varied between 85 and 98%. The immobilized xylanase activity was significantly greater with respect to the free enzyme while the binary enzyme system promoted protease activity.

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