Purification and characterization of a chitosanase fromStreptomycesN174

✍ Scribed by Isabelle Boucher; Agnés Dupuy; Pierre Vidal; Witold A. Neugebauer; Ryszard Brzezinski

• Publisher: Springer
• Year: 1992
• Tongue: English
• Weight: 603 KB
• Volume: 38
• Category: Article
• ISSN: 1432-0614
• DOI: 10.1007/bf00174466

✦ Synopsis

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.