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Purification and characterization of a chitosanase from Streptomyces N174

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Abstract

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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Correspondence to: R. Brzezinski

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Boucher, I., Dupuy, A., Vidal, P. et al. Purification and characterization of a chitosanase from Streptomyces N174. Appl Microbiol Biotechnol 38, 188–193 (1992). https://doi.org/10.1007/BF00174466

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  • DOI: https://doi.org/10.1007/BF00174466

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